Shoulders M. D. ; Raines R. T. Collagen structure and stability . Annu. Rev. Biochem. , 2009 , 78 , 929 - 958 . doi: 10.1146/annurev.biochem.77.032207.120833 http://dx.doi.org/10.1146/annurev.biochem.77.032207.120833

Bielajew B. J. ; Hu J. C. ; Athanasiou K. A. Collagen: Quantification , biomechanics, and role of minor subtypes in cartilage. Nat. Rev. Mater., 2020 , 5 ( 10 ), 730 - 747 . doi: 10.1038/s41578-020-0213-1 http://dx.doi.org/10.1038/s41578-020-0213-1

Brodsky B. ; Ramshaw J. A. M. The collagen triple-helix structure . Matrix Biol. , 1997 , 15 ( 8-9 ), 545 - 554 . doi: 10.1016/s0945-053x(97)90030-5 http://dx.doi.org/10.1016/s0945-053x(97)90030-5

Brodsky B. ; Persikov A. V. Advances in Protein Chemistry: Molecular structure of the collagen triple helix . Vol . 70 . San Diego : Academic Press , 2005. 301 - 339 . doi: 10.1016/s0065-3233(05)70009-7 http://dx.doi.org/10.1016/s0065-3233(05)70009-7

Engel J. ; Bächinger H. P. Structure, stability and folding of the collagen triple helix . Collagen. Berlin, Heidelberg : Springer , 2005 , 7 - 33 . doi: 10.1007/b103818 http://dx.doi.org/10.1007/b103818

Kirkness M. W. ; Lehmann K. ; Forde N. R. Mechanics and structural stability of the collagen triple helix . Curr. Opin. Chem. Biol. , 2019 , 53 , 98 - 105 . doi: 10.1016/j.cbpa.2019.08.001 http://dx.doi.org/10.1016/j.cbpa.2019.08.001

Eastoe J. E. The amino acid composition of mammalian collagen and gelatin . Biochem. J. , 1955 , 61 ( 4 ), 589 - 600 . doi: 10.1042/bj0610589 http://dx.doi.org/10.1042/bj0610589

Li P. ; Wu G. Y. Roles of dietary glycine, proline, and hydroxyproline in collagen synthesis and animal growth . Amino Acids , 2018 , 50 ( 1 ), 29 - 38 . doi: 10.1007/s00726-017-2490-6 http://dx.doi.org/10.1007/s00726-017-2490-6

Ramshaw J. A. M. ; Shah N. K. ; Brodsky B. Gly-X-Y tripeptide frequencies in collagen: a context for host-guest triple-helical peptides . J. Struct. Biol. , 1998 , 122 ( 1-2 ), 86 - 91 . doi: 10.1006/jsbi.1998.3977 http://dx.doi.org/10.1006/jsbi.1998.3977

He L. R. ; Theato P. Collagen and collagen mimetic peptide conjugates in polymer science . Eur. Polym. J. , 2013 , 49 ( 10 ), 2986 - 2997 . doi: 10.1016/j.eurpolymj.2013.05.033 http://dx.doi.org/10.1016/j.eurpolymj.2013.05.033

Zheng M. H. ; Wang X. C. ; Chen Y. N. ; Ouyang Y. ; Bai Z. X. ; Cui B. Q. ; Jiang H. E. ; Liu X. H. A review of recent progress on collagen-based biomaterials . Adv. Healthc. Mater. , 2023 , 12 ( 16 ), 2202042 . doi: 10.1002/adhm.202370080 http://dx.doi.org/10.1002/adhm.202370080

Sionkowska A. ; Adamiak K. ; Musiał K. ; Gadomska M. Collagen based materials in cosmetic applications: a review . Materials , 2020 , 13 ( 19 ), 4217 . doi: 10.3390/ma13194217 http://dx.doi.org/10.3390/ma13194217

Sionkowska A. ; Skrzyński S. ; Śmiechowski K. ; Kołodziejczak A. The review of versatile application of collagen . Polym. Adv. Technol. , 2017 , 28 ( 1 ), 4 - 9 . doi: 10.1002/pat.3842 http://dx.doi.org/10.1002/pat.3842

Shekhter A. B. ; Fayzullin A. L. ; Vukolova M. N. ; Rudenko T. G. ; Osipycheva V. D. ; Litvitsky P. F. Medical applications of collagen and collagen-based materials . Curr. Med. Chem. , 2019 , 26 ( 3 ), 506 - 516 . doi: 10.2174/0929867325666171205170339 http://dx.doi.org/10.2174/0929867325666171205170339

Dong C. J. ; Lv Y. G. Application of collagen scaffold in tissue engineering: recent advances and new perspectives . Polymers , 2016 , 8 ( 2 ), 42 . doi: 10.3390/polym8020042 http://dx.doi.org/10.3390/polym8020042

Lee C. H. ; Singla A. ; Lee Y. Biomedical applications of collagen . Int. J. Pharm. , 2001 , 221 ( 1-2 ), 1 - 22 . doi: 10.1016/s0378-5173(01)00691-3 http://dx.doi.org/10.1016/s0378-5173(01)00691-3

Ann F. ; Simman R. Modern collagen wound dressings: Function and purpose . J. Am. Coll. Certif. Wound Specialists , 2010 , 2 ( 3 ), 50 - 54 . doi: 10.1016/j.jcws.2010.12.003 http://dx.doi.org/10.1016/j.jcws.2010.12.003

Brett D. A review of collagen and collagen-based wound dressings . Wounds , 2008 , 20 ( 12 ), 347 - 356 .

Ge L. M. ; Xu Y. B. ; Li X. Y. ; Yuan L. ; Tan H. ; Li D. F. ; Mu C. D. Fabrication of antibacterial collagen-based composite wound dressing . ACS Sustainable Chem. Eng. , 2018 , 6 ( 7 ), 9153 - 9166 . doi: 10.1021/acssuschemeng.8b01482 http://dx.doi.org/10.1021/acssuschemeng.8b01482

Tang C. ; Zhou K. ; Zhu Y. C. ; Zhang W. D. ; Xie Y. ; Wang Z. M. ; Zhou H. ; Yang T. T. ; Zhang Q. ; Xu B. C. Collagen and its derivatives: from structure and properties to their applications in food industry . Food Hydrocoll. , 2022 , 131 , 107748 . doi: 10.1016/j.foodhyd.2022.107748 http://dx.doi.org/10.1016/j.foodhyd.2022.107748

Hu X. ; Wu Z. L. ; Zhang Z. ; Yao H. ; Wang D. A. Type II collagen scaffolds for tissue engineering . Commun. Mater. , 2024 , 5 , 149 . doi: 10.1038/s43246-024-00598-x http://dx.doi.org/10.1038/s43246-024-00598-x

Rezvani Ghomi E. ; Nourbakhsh N. ; Akbari Kenari M. ; Zare M. ; Ramakrishna S. Collagen-based biomaterials for biomedical applications . J. Biomed. Mater. Res. B Appl. Biomater. , 2021 , 109 ( 12 ), 1986 - 1999 . doi: 10.1002/jbm.b.34881 http://dx.doi.org/10.1002/jbm.b.34881

Coppola D. ; Oliviero M. ; Vitale G. A. ; Lauritano C. ; D'Ambra I. ; Iannace S. ; de Pascale D. Marine collagen from alternative and sustainable sources: extraction, processing and applications . Mar. Drugs , 2020 , 18 ( 4 ), 214 . doi: 10.3390/md18040214 http://dx.doi.org/10.3390/md18040214

Ahmed M. ; Verma A. K. ; Patel R. Collagen extraction and recent biological activities of collagen peptides derived from sea-food waste: a review . Sustain. Chem. Pharm. , 2020 , 18 , 100315 . doi: 10.1016/j.scp.2020.100315 http://dx.doi.org/10.1016/j.scp.2020.100315

Matinong A. M. E. ; Chisti Y. ; Pickering K. L. ; Haverkamp R. G. Collagen extraction from animal skin . Biology , 2022 , 11 ( 6 ), 905 . doi: 10.3390/biology11060905 http://dx.doi.org/10.3390/biology11060905

Wang T. Y. ; Lew J. ; Premkumar J. ; Poh C. L. ; Win Naing M. Production of recombinant collagen: state of the art and challenges . Eng. Biol. , 2017 , 1 ( 1 ), 18 - 23 . doi: 10.1049/enb.2017.0003 http://dx.doi.org/10.1049/enb.2017.0003

Olsen D. ; Yang C. L. ; Bodo M. ; Chang R. ; Leigh S. ; Baez J. ; Carmichael D. ; Perälä M. ; Hämäläinen E. R. ; Jarvinen M. ; Polarek J. Recombinant collagen and gelatin for drug delivery . Adv. Drug Deliv. Rev. , 2003 , 55 ( 12 ), 1547 - 1567 . doi: 10.1016/j.addr.2003.08.008 http://dx.doi.org/10.1016/j.addr.2003.08.008

Báez J. ; Olsen D. ; Polarek J. W. Recombinant microbial systems for the production of human collagen and gelatin . Appl. Microbiol. Biotechnol. , 2005 , 69 ( 3 ), 245 - 252 . doi: 10.1007/s00253-005-0180-x http://dx.doi.org/10.1007/s00253-005-0180-x

Yang C. L. ; Hillas P. J. ; Báez J. A. ; Nokelainen M. ; Balan J. ; Tang J. ; Spiro R. ; Polarek J. W. The application of recombinant human collagen in tissue engineering . BioDrugs , 2004 , 18 ( 2 ), 103 - 119 . doi: 10.2165/00063030-200418020-00004 http://dx.doi.org/10.2165/00063030-200418020-00004

Rutschmann C. ; Baumann S. ; Cabalzar J. ; Luther K. B. ; Hennet T. Recombinant expression of hydroxylated human collagen in Escherichia coli . Appl. Microbiol. Biotechnol. , 2014 , 98 ( 10 ), 4445 - 4455 . doi: 10.1007/s00253-013-5447-z http://dx.doi.org/10.1007/s00253-013-5447-z

An B. ; Kaplan D. L. ; Brodsky B. Engineered recombinant bacterial collagen as an alternative collagen-based biomaterial for tissue engineering . Front. Chem. , 2014 , 2 , 40 . doi: 10.3389/fchem.2014.00040 http://dx.doi.org/10.3389/fchem.2014.00040

Bou-Gharios, G.; de Crombrugghe, B. Type I collagen structure, synthesis, and regulation . In Principles of Bone Biology , 3rd ed . ; Bilezikian, J. P., Raisz, L. G., Martin, T. J., Eds.; San Diego : Academic Press , 2008 ; pp 285 - 318 . doi: 10.1016/b978-0-12-373884-4.00034-3 http://dx.doi.org/10.1016/b978-0-12-373884-4.00034-3

Shi J. J. ; Ma X. X. ; Gao Y. ; Fan D. D. ; Zhu C. H. ; Mi Y. ; Xue W. J. Hydroxylation of human type III collagen alpha chain by recombinant coexpression with a viral prolyl 4-hydroxylase in escherichia coli . Protein J. , 2017 , 36 ( 4 ), 322 - 331 . doi: 10.1007/s10930-017-9723-0 http://dx.doi.org/10.1007/s10930-017-9723-0

Xu Y. J. ; Kirchner , M. Collagen mimetic peptides . Bioengineering , 2021 , 8 ( 1 ), 5 . doi: 10.3390/bioengineering8010005 http://dx.doi.org/10.3390/bioengineering8010005

Hulgan S. A. H. ; Hartgerink J. D. Recent advances in collagen mimetic peptide structure and design . Biomacromolecules , 2022 , 23 ( 4 ), 1475 - 1489 . doi: 10.1021/acs.biomac.2c00028 http://dx.doi.org/10.1021/acs.biomac.2c00028

Shi L. Q. ; Holliday A. E. ; Shi H. L. ; Zhu F. F. ; Ewing M. A. ; Russell D. H. ; Clemmer D. E. Characterizing intermediates along the transition from polyproline I to polyproline II using ion mobility spectrometry-mass spectrometry . J. Am. Chem. Soc. , 2014 , 136 ( 36 ), 12702 - 12711 . doi: 10.1021/ja505899g http://dx.doi.org/10.1021/ja505899g

Forsythe K. H. ; Hopfinger A. J. The influence of solvent on the secondary structures of poly(L-alanine) and poly(L-proline) . Macromolecules , 1973 , 6 ( 3 ), 423 - 437 . doi: 10.1021/ma60033a020 http://dx.doi.org/10.1021/ma60033a020

Steinberg I. Z. ; Harrington W. F. ; Berger A. ; Sela M. ; Katchalski E. The configurational changes of poly-L-proline in solution . J. Am. Chem. Soc. , 1960 , 82 ( 20 ), 5263 - 5279 . doi: 10.1021/ja01505a001 http://dx.doi.org/10.1021/ja01505a001

Kodr D. ; Fiala T. ; Wennemers H. The irreplaceable glycine: glycine homologs destabilize the collagen triple helix . Tetrahedron Lett. , 2024 , 138 , 154964 . doi: 10.1016/j.tetlet.2024.154964 http://dx.doi.org/10.1016/j.tetlet.2024.154964

Yang J. Y. ; Kojasoy V. ; Porter G. J. ; Raines R. T. Pauli exclusion by n→ π * interactions: implications for paleobiology . ACS Cent. Sci. , 2024 , 10 ( 10 ), 1829 - 1834 . doi: 10.1021/acscentsci.4c00971 http://dx.doi.org/10.1021/acscentsci.4c00971

Fratzl P. ; Misof K. ; Zizak I. ; Rapp G. ; Amenitsch H. ; Bernstorff S. Fibrillar structure and mechanical properties of collagen . J. Struct. Biol. , 1998 , 122 ( 1-2 ), 119 - 122 . doi: 10.1006/jsbi.1998.3966 http://dx.doi.org/10.1006/jsbi.1998.3966

Wenger M. P. E. ; Bozec L. ; Horton M. A. ; Mesquida P. Mechanical properties of collagen fibrils . Biophys. J. , 2007 , 93 ( 4 ), 1255 - 1263 . doi: 10.1529/biophysj.106.103192 http://dx.doi.org/10.1529/biophysj.106.103192

Kato Y. P. ; Christiansen D. L. ; Hahn R. A. ; Shieh S. J. ; Goldstein J. D. ; Silver F. H. Mechanical properties of collagen fibres: a comparison of reconstituted and rat tail tendon fibres . Biomaterials , 1989 , 10 ( 1 ), 38 - 42 . doi: 10.1016/0142-9612(89)90007-0 http://dx.doi.org/10.1016/0142-9612(89)90007-0

Couppé C. ; Hansen P. ; Kongsgaard M. ; Kovanen V. ; Suetta C. ; Aagaard P. ; Kjaer M. ; Magnusson S. P. Mechanical properties and collagen cross-linking of the patellar tendon in old and young men . J. Appl. Physiol. , 2009 , 107 ( 3 ), 880 - 886 . doi: 10.1152/japplphysiol.00291.2009 http://dx.doi.org/10.1152/japplphysiol.00291.2009

Sakakibara S. ; Inouye K. ; Shudo K. ; Kishida Y. ; Kobayashi Y. ; Prockop D. J. Synthesis of (Pro-Hyp-Gly) n of defined molecular weights evidence for the stabilization of collagen triple helix by hydroxypyroline . Biochim. Biophys. Acta BBA Protein Struct. , 1973 , 303 ( 1 ), 198 - 202 . doi: 10.1016/0005-2795(73)90164-5 http://dx.doi.org/10.1016/0005-2795(73)90164-5

Sutoh K. ; Noda H. Conformational change of the triple-helical structure . IV. Kinetics of the helix-folding of (Pro-Pro-Gly)n (n= 10 , 12 , and 15 ). Biopolymers, 1974, 13 ( 12 ), 2477 - 2488 . doi: 10.1002/bip.1974.360131207 http://dx.doi.org/10.1002/bip.1974.360131207

Fields G. B. ; Prockop D. J. Perspectives on the synthesis and application of triple-helical, collagen-model peptides . Biopolymers , 1996 , 40 ( 4 ), 345 - 357 . doi: 10.1002/(sici)1097-0282(1996)40:4<345::aid-bip1>3.3.co;2-# http://dx.doi.org/10.1002/(sici)1097-0282(1996)40:4<345::aid-bip1>3.3.co;2-#

Brodsky B. ; Thiagarajan G. ; Madhan B. ; Kar K. Triple-helical peptides: an approach to collagen conformation, stability, and self-association . Biopolymers , 2008 , 89 ( 5 ), 345 - 353 . doi: 10.1002/bip.20958 http://dx.doi.org/10.1002/bip.20958

Buevich A. V. ; Silva T. ; Brodsky B. ; Baum J. Transformation of the mechanism of triple-helix peptide folding in the absence of a C-terminal nucleation domain and its implications for mutations in collagen disorders . J. Biol. Chem. , 2004 , 279 ( 45 ), 46890 - 46895 . doi: 10.1074/jbc.m407061200 http://dx.doi.org/10.1074/jbc.m407061200

Hyde T. J. ; Bryan M. A. ; Brodsky B. ; Baum J. Sequence dependence of renucleation after a Gly mutation in model collagen peptides . J. Biol. Chem. , 2006 , 281 ( 48 ), 36937 - 36943 . doi: 10.1074/jbc.m605135200 http://dx.doi.org/10.1074/jbc.m605135200

Xu Y. J. ; Bhate M. ; Brodsky B. Characterization of the nucleation step and folding of a collagen triple-helix peptide . Biochemistry , 2002 , 41 ( 25 ), 8143 - 8151 . doi: 10.1021/bi015952b http://dx.doi.org/10.1021/bi015952b

Egli J. ; Erdmann R. S. ; Schmidt P. J. ; Wennemers H. Effect of N- and C-terminal functional groups on the stability of collagen triple helices . Chem. Commun. , 2017 , 53 ( 80 ), 11036 - 11039 . doi: 10.1039/c7cc05837c http://dx.doi.org/10.1039/c7cc05837c

Qi Y. Y. ; Zhou D. N. ; Kessler J. L. ; Qiu R. M. ; Yu S. M. ; Li G. ; Qin Z. ; Li Y. Terminal repeats impact collagen triple-helix stability through hydrogen bonding . Chem. Sci. , 2022 , 13 ( 42 ), 12567 - 12576 . doi: 10.1039/d2sc03666e http://dx.doi.org/10.1039/d2sc03666e

Fiala T. ; Barros E. P. ; Heeb R. ; Riniker S. ; Wennemers H. Predicting collagen triple helix stability through additive effects of terminal residues and caps . Angew. Chem. Int. Ed. , 2023 , 62 ( 3 ), e 202214728 . doi: 10.1002/anie.202214728 http://dx.doi.org/10.1002/anie.202214728

Fiala T. ; Barros E. P. ; Ebert M. O. ; Ruijsenaars E. ; Riniker S. ; Wennemers H. Frame shifts affect the stability of collagen triple helices . J. Am. Chem. Soc. , 2022 , 144 ( 40 ), 18642 - 18649 . doi: 10.1021/jacs.2c08727 http://dx.doi.org/10.1021/jacs.2c08727

Chiu H. S. ; Horng J. C. Modulating the stability of collagen triple helices by terminal charged residues . J. Phys. Chem. B , 2021 , 125 ( 27 ), 7351 - 7358 . doi: 10.1021/acs.jpcb.1c01631 http://dx.doi.org/10.1021/acs.jpcb.1c01631

Acevedo-Jake A. M. ; Jalan A. A. ; Hartgerink J. D. Comparative NMR analysis of collagen triple helix organization from N- to C-termini . Biomacromolecules , 2015 , 16 ( 1 ), 145 - 155 . doi: 10.1021/bm501281a http://dx.doi.org/10.1021/bm501281a

Kishimoto T. ; Morihara Y. ; Osanai M. ; Ogata S. I. ; Kamitakahara M. ; Ohtsuki C. ; Tanihara M. Synthesis of poly(Pro-Hyp-Gly) n by direct poly-condensation of (Pro-Hyp-Gly) n , where n= 1 , 5 , and 10 , and stability of the triple-helical structure. Biopolymers, 2005, 79 ( 3 ), 163 - 172 . doi: 10.1002/bip.20348 http://dx.doi.org/10.1002/bip.20348

Kubyshkin V. ; Rubini , M. Proline analogues . Chem. Rev. , 2024 , 124 ( 13 ), 8130 - 8232 . doi: 10.1021/acs.chemrev.4c00007 http://dx.doi.org/10.1021/acs.chemrev.4c00007

Holmgren S. K. ; Taylor K. M. ; Bretscher L. E. ; Raines R. T. Code for collagen's stability deciphered . Nature , 1998 , 392 ( 6677 ), 666 - 667 . doi: 10.1038/33573 http://dx.doi.org/10.1038/33573

Bretscher L. E. ; Jenkins C. L. ; Taylor K. M. ; DeRider M. L. ; Raines R. T. Conformational stability of collagen relies on a stereoelectronic effect . J. Am. Chem. Soc. , 2001 , 123 ( 4 ), 777 - 778 . doi: 10.1021/ja005542v http://dx.doi.org/10.1021/ja005542v

DeRider M. L. ; Wilkens S. J. ; Waddell M. J. ; Bretscher L. E. ; Weinhold F. ; Raines R. T. ; Markley J. L. Collagen stability: insights from NMR spectroscopic and hybrid density functional computational investigations of the effect of electronegative substituents on prolyl ring conformations . J. Am. Chem. Soc. , 2002 , 124 ( 11 ), 2497 - 2505 . doi: 10.1021/ja0166904 http://dx.doi.org/10.1021/ja0166904

Hodges J. A. ; Raines R. T. Stereoelectronic effects on collagen stability: the dichotomy of 4-fluoroproline diastereomers . J. Am. Chem. Soc. , 2003 , 125 ( 31 ), 9262 - 9263 . doi: 10.1021/ja035881z http://dx.doi.org/10.1021/ja035881z

Egli J. ; Siebler C. ; Maryasin B. ; Erdmann R. S. ; Bergande C. ; Ochsenfeld C. ; Wennemers H. pH-responsive aminoproline-containing collagen triple helices . Chem. , 2017 , 23 ( 33 ), 7938 - 7944 . doi: 10.1002/chem.201701134 http://dx.doi.org/10.1002/chem.201701134

Siebler C. ; Erdmann R. S. ; Wennemers H. Switchable proline derivatives: tuning the conformational stability of the collagen triple helix by pH changes . Angew. Chem. Int. Ed. , 2014 , 53 ( 39 ), 10340 - 10344 . doi: 10.1002/anie.201404935 http://dx.doi.org/10.1002/anie.201404935

Aronoff M. R. ; Egli J. ; Menichelli M. ; Wennemers H. γ -azaproline confers pH Responsiveness and functionalizability on collagen triple helices . Angew. Chem. Int. Ed. , 2019 , 58 ( 10 ), 3143 - 3146 . doi: 10.1002/anie.201813048 http://dx.doi.org/10.1002/anie.201813048

Aronoff M. R. ; Egli J. ; Schmitt A. ; Wennemers H. Alkylation of γ -azaproline creates conformationally adaptable proline derivatives for pH-responsive collagen triple helices . Chemistry , 2020 , 26 ( 22 ), 5070 - 5074 . doi: 10.1002/chem.201905768 http://dx.doi.org/10.1002/chem.201905768

Terrien A. ; Rahgoshay K. ; Renaglia E. ; Lensen N. ; Jacquot Y. ; Marquant R. ; Brigaud T. ; Loison C. ; Chaume G. ; Miclet E. Inviting C5-trifluoromethylated pseudoprolines into collagen mimetic peptides . Biomacromolecules , 2023 , 24 ( 4 ), 1555 - 1562 . doi: 10.1021/acs.biomac.2c01242 http://dx.doi.org/10.1021/acs.biomac.2c01242

Egli J. ; Schnitzer T. ; Dietschreit J. C. B. ; Ochsenfeld C. ; Wennemers H. Why proline? Influence of ring-size on the collagen triple helix . Org. Lett. , 2020 , 22 ( 2 ), 348 - 351 . doi: 10.1021/acs.orglett.9b03528 http://dx.doi.org/10.1021/acs.orglett.9b03528

Harris T. ; Chenoweth D. M. Sterics and stereoelectronics in aza-glycine: impact of aza-glycine preorganization in triple helical collagen . J. Am. Chem. Soc. , 2019 , 141 ( 45 ), 18021 - 18029 . doi: 10.1021/jacs.9b05524 http://dx.doi.org/10.1021/jacs.9b05524

Zhang Y. T. ; Malamakal R. M. ; Chenoweth D. M. Aza-glycine induces collagen hyperstability . J. Am. Chem. Soc. , 2015 , 137 ( 39 ), 12422 - 12425 . doi: 10.1021/jacs.5b04590 http://dx.doi.org/10.1021/jacs.5b04590

Zhang Y. T. ; Herling M. ; Chenoweth D. M. General solution for stabilizing triple helical collagen . J. Am. Chem. Soc. , 2016 , 138 ( 31 ), 9751 - 9754 . doi: 10.1021/jacs.6b03823 http://dx.doi.org/10.1021/jacs.6b03823

Kasznel A. J. ; Zhang Y. T. ; Hai Y. ; Chenoweth D. M. Structural basis for aza-glycine stabilization of collagen . J. Am. Chem. Soc. , 2017 , 139 ( 28 ), 9427 - 9430 . doi: 10.1021/jacs.7b03398 http://dx.doi.org/10.1021/jacs.7b03398

Hentzen N. B. ; Smeenk L. E. J. ; Witek J. ; Riniker S. ; Wennemers H. Cross-linked collagen triple helices by oxime ligation . J. Am. Chem. Soc. , 2017 , 139 ( 36 ), 12815 - 12820 . doi: 10.1021/jacs.7b07498 http://dx.doi.org/10.1021/jacs.7b07498

Hentzen N. B. ; Islami V. ; Köhler M. ; Zenobi R. ; Wennemers H. A lateral salt bridge for the specific assembly of an ABC-type collagen heterotrimer . J. Am. Chem. Soc. , 2020 , 142 ( 5 ), 2208 - 2212 . doi: 10.1021/jacs.9b13037 http://dx.doi.org/10.1021/jacs.9b13037

Egli J. ; Esposito C. ; Müri M. ; Riniker S. ; Wennemers H. Influence of lipidation on the folding and stability of collagen triple helices: an experimental and theoretical study . J. Am. Chem. Soc. , 2021 , 143 ( 15 ), 5937 - 5942 . doi: 10.1021/jacs.1c01512 http://dx.doi.org/10.1021/jacs.1c01512

Malcor J. D. ; Ferruz N. ; Romero-Romero S. ; Dhingra S. ; Sagar V. ; Jalan A. A. Deciphering the folding code of collagens . Nat. Commun. , 2025 , 16 ( 1 ), 2702 . doi: 10.1038/s41467-024-54046-y http://dx.doi.org/10.1038/s41467-024-54046-y

Chen C. C. ; Hsu W. ; Hwang K. C. ; Hwu J. R. ; Lin C. C. ; Horng J. C. Contributions of cation- π interactions to the collagen triple helix stability . Arch. Biochem. Biophys. , 2011 , 508 ( 1 ), 46 - 53 . doi: 10.1016/j.abb.2011.01.009 http://dx.doi.org/10.1016/j.abb.2011.01.009

Persikov A. V. ; Xu Y. J. ; Brodsky B. Equilibrium thermal transitions of collagen model peptides . Protein Sci. , 2004 , 13 ( 4 ), 893 - 902 . doi: 10.1110/ps.03501704 http://dx.doi.org/10.1110/ps.03501704

Persikov A. V. ; Ramshaw J. A. M. ; Brodsky B. Prediction of collagen stability from amino acid sequence . J. Biol. Chem. , 2005 , 280 ( 19 ), 19343 - 19349 . doi: 10.1074/jbc.m501657200 http://dx.doi.org/10.1074/jbc.m501657200

Persikov A. V. ; Ramshaw J. A. M. ; Kirkpatrick A. ; Brodsky B. Electrostatic interactions involving lysine make major contributions to collagen triple-helix stability . Biochemistry , 2005 , 44 ( 5 ), 1414 - 1422 . doi: 10.1021/bi048216r http://dx.doi.org/10.1021/bi048216r

Persikov A. V. ; Ramshaw J. A. ; Kirkpatrick A. ; Brodsky B. Amino acid propensities for the collagen triple-helix . Biochemistry , 2000 , 39 ( 48 ), 14960 - 14967 . doi: 10.1021/bi001560d http://dx.doi.org/10.1021/bi001560d

Persikov A. V. ; Ramshaw J. A. M. ; Kirkpatrick A. ; Brodsky B. Peptide investigations of pairwise interactions in the collagen triple-helix . J. Mol. Biol. , 2002 , 316 ( 2 ), 385 - 394 . doi: 10.1006/jmbi.2001.5342 http://dx.doi.org/10.1006/jmbi.2001.5342

Chen L. W. ; Cai S. T. ; Lim J. ; Lee S. S. ; Lee S. G. Elucidating pH-dependent collagen triple helix formation through interstrand hydroxyproline-glutamic acid interactions . ChemBioChem , 2015 , 16 ( 3 ), 407 - 410 . doi: 10.1002/cbic.201402570 http://dx.doi.org/10.1002/cbic.201402570

Kramer R. Z. ; Venugopal M. G. ; Bella J. ; Mayville P. ; Brodsky B. ; Berman H. M. Staggered molecular packing in crystals of a collagen-like peptide with a single charged pair 1 . J. Mol. Biol. , 2000 , 301 ( 5 ), 1191 - 1205 . doi: 10.1006/jmbi.2000.4017 http://dx.doi.org/10.1006/jmbi.2000.4017

Fallas J. A. ; Hartgerink J. D. Computational design of self-assembling register-specific collagen heterotrimers . Nat. Commun. , 2012 , 3 , 1087 . doi: 10.1038/ncomms2084 http://dx.doi.org/10.1038/ncomms2084

Fallas J. A. ; Lee M. A. ; Jalan A. A. ; Hartgerink J. D. Rational design of single-composition ABC collagen heterotrimers . J. Am. Chem. Soc. , 2012 , 134 ( 3 ), 1430 - 1433 . doi: 10.1021/ja209669u http://dx.doi.org/10.1021/ja209669u

Jalan A. A. ; Demeler B. ; Hartgerink J. D. Hydroxyproline-free single composition ABC collagen heterotrimer . J. Am. Chem. Soc. , 2013 , 135 ( 16 ), 6014 - 6017 . doi: 10.1021/ja402187t http://dx.doi.org/10.1021/ja402187t

O'Leary L. E. R. ; Fallas J. A. ; Hartgerink J. D. Positive and negative design leads to compositional control in AAB collagen heterotrimers . J. Am. Chem. Soc. , 2011 , 133 ( 14 ), 5432 - 5443 . doi: 10.1021/ja111239r http://dx.doi.org/10.1021/ja111239r

Russell L. E. ; Fallas J. A. ; Hartgerink J. D. Selective assembly of a high stability AAB collagen heterotrimer . J. Am. Chem. Soc. , 2010 , 132 ( 10 ), 3242 - 3243 . doi: 10.1021/ja909720g http://dx.doi.org/10.1021/ja909720g

Zheng H. N. ; Lu C. ; Lan J. ; Fan S. L. ; Nanda V. ; Xu F. How electrostatic networks modulate specificity and stability of collagen . Proc. Natl. Acad. Sci. USA , 2018 , 115 ( 24 ), 6207 - 6212 . doi: 10.1073/pnas.1802171115 http://dx.doi.org/10.1073/pnas.1802171115

Jalan A. A. ; Sammon D. ; Hartgerink J. D. ; Brear P. ; Stott K. ; Hamaia S. W. ; Hunter E. J. ; Walker D. R. ; Leitinger B. ; Farndale R. W. Chain alignment of collagen I deciphered using computationally designed heterotrimers . Nat. Chem. Biol. , 2020 , 16 ( 4 ), 423 - 429 . doi: 10.1038/s41589-019-0435-y http://dx.doi.org/10.1038/s41589-019-0435-y

Zheng H. N. ; Liu H. ; Hu J. Y. ; Xu F. Using a collagen heterotrimer to screen for cation- π interactions to stabilize triple helices . Chem. Phys. Lett. , 2019 , 715 , 77 - 83 . doi: 10.1016/j.cplett.2018.10.073 http://dx.doi.org/10.1016/j.cplett.2018.10.073

Gauba V. ; Hartgerink J. D. Surprisingly high stability of collagen ABC heterotrimer: evaluation of side chain charge pairs . J. Am. Chem. Soc. , 2007 , 129 ( 48 ), 15034 - 15041 . doi: 10.1021/ja075854z http://dx.doi.org/10.1021/ja075854z

O'Leary L. E. R. ; Fallas J. A. ; Bakota E. L. ; Kang M. K. ; Hartgerink J. D. Multi-hierarchical self-assembly of a collagen mimetic peptide from triple helix to nanofibre and hydrogel . Nat. Chem. , 2011 , 3 ( 10 ), 821 - 828 . doi: 10.1038/nchem.1123 http://dx.doi.org/10.1038/nchem.1123

Tanrikulu I. C. ; Forticaux A. ; Jin S. ; Raines R. T. Peptide tessellation yields micrometre-scale collagen triple helices . Nat. Chem. , 2016 , 8 ( 11 ), 1008 - 1014 . doi: 10.1038/nchem.2556 http://dx.doi.org/10.1038/nchem.2556

Walker D. R. ; Alizadehmojarad A. A. ; Kolomeisky A. B. ; Hartgerink J. D. Charge-free, stabilizing amide- π interactions can be used to control collagen triple-helix self-assembly . Biomacromolecules , 2021 , 22 ( 5 ), 2137 - 2147 . doi: 10.1021/acs.biomac.1c00234 http://dx.doi.org/10.1021/acs.biomac.1c00234

Rasines Mazo A. ; Allison-Logan S. ; Karimi F. ; Chan N. J. ; Qiu W. L. ; Duan W. ; O'Brien-Simpson N. M. ; Qiao G. G. Ring opening polymerization of α -amino acids: advances in synthesis, architecture and applications of polypeptides and their hybrids . Chem. Soc. Rev. , 2020 , 49 ( 14 ), 4737 - 4834 . doi: 10.1039/c9cs00738e http://dx.doi.org/10.1039/c9cs00738e

Lu H. ; Wang J. ; Song Z. Y. ; Yin L. C. ; Zhang Y. F. ; Tang H. Y. ; Tu C. L. ; Lin Y. ; Cheng J. J. Recent advances in amino acid N -carb oxyanhydrides and synthetic polypeptides: chemistry, self-assembly and biological applications . Chem. Commun. , 2014 , 50 ( 2 ), 139 - 155 . doi: 10.1039/c3cc46317f http://dx.doi.org/10.1039/c3cc46317f

Deming T. J. Polypeptide and polypeptide hybrid copolymer synthesis via NCA polymerization . in Peptide Hybrid Polymers. Berlin/Heidelberg : Springer-Verlag , 2006 , 1 - 18 . doi: 10.1002/chin.200705228 http://dx.doi.org/10.1002/chin.200705228

Hadjichristidis N. ; Iatrou H. ; Pitsikalis M. ; Sakellariou G. Synthesis of well-defined polypeptide-based materials via the ring-opening polymerization of α -amino acid N -carboxyanhydrides . Chem. Rev. , 2009 , 109 ( 11 ), 5528 - 5578 . doi: 10.1021/cr900049t http://dx.doi.org/10.1021/cr900049t

Yu X. Y. ; Wang Y. ; Dong Y. T. ; Zhao N. ; Zhang L. F. ; Xuan S. T. ; Zhang Z. B. Efficient synthesis of N -methyl polypeptides by organic acid promoted controlled ring-opening polymerization of N -methyl- α -amino acids N -carboxyanhydrides . Macromolecules , 2023 , 56 ( 21 ), 8899 - 8911 . doi: 10.1021/acs.macromol.3c01102 http://dx.doi.org/10.1021/acs.macromol.3c01102

Liu X. L. ; Huang J. ; Wang J. Q. ; Sheng H. N. ; Yuan Z. ; Wang W. Y. ; Li W. B. ; Song Z. Y. ; Cheng J. J. Accelerated and controlled polymerization of N -carboxyanhydrides assisted by acids . CCS Chem. , 2025 , 7 ( 9 ), 2769 - 2780 . doi: 10.31635/ccschem.024.202403954 http://dx.doi.org/10.31635/ccschem.024.202403954

漆李矜 , 黄琪杨 , 高晴妤 , 韩笛 , 廖馨茹 , 张先正 , 程巳雪 . 氨基酸基材料在基因与药物传递领域的应用 . 高分子学报 , 2025 , 56 ( 1 ), 1 - 25 .

滕润鑫 , 范震 , 杜建忠 . 肿瘤诊疗多肽/聚氨基酸自组装纳米材料 . 高分子学报 , 2023 , 54 ( 6 ), 853 - 869 .

张冲 , 吕华 . 蛋白质-聚氨基酸偶联物的高效合成与应用 . 高分子学报 , 2018 , ( 1 ), 21 - 31 .

Berger A. ; Kurtz J. ; Katchalski E. Poly-L-proline . J. Am. Chem. Soc. , 1954 , 76 ( 21 ), 5552 - 5554 . doi: 10.1021/ja01650a082 http://dx.doi.org/10.1021/ja01650a082

Kurtz J. ; Fasman G. D. ; Berger A. ; Katchalski E. Poly-hydroxy- L -proline . J. Am. Chem. Soc. , 1958 , 80 ( 2 ), 393 - 397 . doi: 10.1021/ja01535a037 http://dx.doi.org/10.1021/ja01535a037

Detwiler R. E. ; Schlirf A. E. ; Kramer J. R. Rethinking transition metal catalyzed N -carboxyanhydride polymerization: polymerization of pro and AcOPro N -carboxyanhydrides . J. Am. Chem. Soc. , 2021 , 143 ( 30 ), 11482 - 11489 . doi: 10.1021/jacs.1c03338 http://dx.doi.org/10.1021/jacs.1c03338

Hu Y. L. ; Tian Z. Y. ; Xiong W. ; Wang D. D. ; Zhao R. C. ; Xie Y. ; Song Y. Q. ; Zhu J. ; Lu H. Water-assisted and protein-initiated fast and controlled ring-opening polymerization of proline N -carboxyanhydride . Natl. Sci. Rev. , 2022 , 9 ( 8 ), nwac 033 . doi: 10.1093/nsr/nwac033 http://dx.doi.org/10.1093/nsr/nwac033

Zhao R. C. ; Zhang Y. M. ; Ruan B. L. ; Zhang H. R. ; Lv N. N. ; Li J. Y. ; Yang Y. R. ; Luo X. Z. ; Lu H. Nanourchin-like uricase-poly((L)-proline) conjugate with retained enzymatic activity , mitigated immunogenicity, and sustained efficacy upon repeated administrations. Angew. Chem. Int. Ed., 2025 , 64 ( 20 ), e 202425559 . doi: 10.1002/anie.202425559 http://dx.doi.org/10.1002/anie.202425559

Tian Z. Y. ; Zhang Z. C. ; Wang S. ; Lu H. A moisture-tolerant route to unprotected α / β -amino acid N -carboxyanhydrides and facile synthesis of hyperbranched polypeptides . Nat. Commun. , 2021 , 12 ( 1 ), 5810 . doi: 10.1038/s41467-021-25689-y http://dx.doi.org/10.1038/s41467-021-25689-y

Wang L. T. ; Wang W. C. ; Zhu X. Y. ; Tang C. M. ; Jing X. D. ; He Y. H. ; Amengual J. ; Lin Y. ; Yu Z. X. ; Lu H. Ring-opening polymerization of unprotected hydroxyproline N -carboxyanhydride for the facile synthesis of linear and branched poly-l-hydroxyproline . CCS Chem. , 2025 , 7 ( 12 ), 3807 - 3822 . doi: 10.31635/ccschem.025.202506277 http://dx.doi.org/10.31635/ccschem.025.202506277