Conformational Analysis of Fluoro-, Chloro-, and Proteo-Alkene Gly-Pro and Pro-Pro Isosteres to Mimic Collagen

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dc.contributor.authorArcoria, Paul J.en
dc.contributor.authorWare, Rachel I.en
dc.contributor.authorMakwana, Sunny V.en
dc.contributor.authorTroya, Diegoen
dc.contributor.authorEtzkorn, Felicia A.en
dc.date.accessioned2022-01-14T18:18:23Zen
dc.date.available2022-01-14T18:18:23Zen
dc.date.issued2021-12-30en
dc.date.updated2022-01-14T18:18:19Zen
dc.description.abstractCollagen is the most abundant human protein, with the canonical sequence (Gly-Pro-Hyp)<i><sub>n</sub></i> in its triple helix region. Cis-trans isomerization of the Xaa-Pro amide has made two of these amide bonds the target of alkene replacement: the Gly-Pro and the Pro-Hyp positions. The conformations of Gly-Pro and Pro-Pro (as a Pro-Hyp model) fluoro-, chloro-, and proteo-alkene mimic models were investigated computationally to determine whether these alkenes can stabilize the polyproline type II (PPII) conformation of collagen. Second-order Møller-Plesset (MP2) calculations with various basis sets were used to perform the conformational analyses and locate stationary points. The calculation results predict that fluoro- and chloro-alkene mimics of Gly-Pro and Pro-Pro can participate in n→π* donation to stabilize PPII conformations, yet they are poor n→π* acceptors, shifting the global minima away from PPII conformations. For the proteo-alkene mimics, the lack of significant n→π* interactions and unstable PPII-like geometries explains their known destabilization of the triple helix in collagen-like peptides.en
dc.description.versionAccepted versionen
dc.format.mimetypeapplication/pdfen
dc.identifieracs.jpcb.1c09180 (Article number)en
dc.identifier.doihttps://doi.org/10.1021/acs.jpcb.1c09180en
dc.identifier.eissn1520-5207en
dc.identifier.issn1520-6106en
dc.identifier.orcidEtzkorn, Felicia [0000-0001-5850-3661]en
dc.identifier.orcidTroya, Diego [0000-0003-4971-4998]en
dc.identifier.pmid34968406en
dc.identifier.urihttp://hdl.handle.net/10919/107643en
dc.language.isoenen
dc.publisherAmerican Chemical Societyen
dc.relation.urihttps://www.ncbi.nlm.nih.gov/pubmed/34968406en
dc.rightsIn Copyrighten
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/en
dc.subject02 Physical Sciencesen
dc.subject03 Chemical Sciencesen
dc.subject09 Engineeringen
dc.titleConformational Analysis of Fluoro-, Chloro-, and Proteo-Alkene Gly-Pro and Pro-Pro Isosteres to Mimic Collagenen
dc.title.serialThe Journal of Physical Chemistry. Ben
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten
dc.type.otherJournal Articleen
pubs.organisational-group/Virginia Techen
pubs.organisational-group/Virginia Tech/Scienceen
pubs.organisational-group/Virginia Tech/Science/Chemistryen
pubs.organisational-group/Virginia Tech/University Research Institutesen
pubs.organisational-group/Virginia Tech/University Research Institutes/Fralin Life Sciencesen
pubs.organisational-group/Virginia Tech/Faculty of Health Sciencesen
pubs.organisational-group/Virginia Tech/All T&R Facultyen
pubs.organisational-group/Virginia Tech/Science/COS T&R Facultyen
pubs.organisational-group/Virginia Tech/University Research Institutes/Fralin Life Sciences/Durelle Scotten

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