DC Field | Value | Language |
---|---|---|
dc.contributor.author | Alarcon, Emilio I. | ko |
dc.contributor.author | Poblete, Horacio | ko |
dc.contributor.author | Roh, HeeGwang | ko |
dc.contributor.author | Couture, Jean-Francois | ko |
dc.contributor.author | Comer, Jeffrey | ko |
dc.contributor.author | Kochevar, Irene E. | ko |
dc.date.accessioned | 2018-02-21T05:26:15Z | - |
dc.date.available | 2018-02-21T05:26:15Z | - |
dc.date.created | 2018-01-15 | - |
dc.date.created | 2018-01-15 | - |
dc.date.created | 2018-01-15 | - |
dc.date.issued | 2017-10 | - |
dc.identifier.citation | ACS OMEGA, v.2, no.10, pp.6646 - 6657 | - |
dc.identifier.issn | 2470-1343 | - |
dc.identifier.uri | http://hdl.handle.net/10203/240050 | - |
dc.description.abstract | We investigated two critical aspects of rose Bengal (RB) photosensitized protein cross-linking that may underlie recently developed medical applications. Our studies focused on the binding of RB to collagen by physical interaction and the effect of this binding and certain amino acids on RB photochemistry. Molecular dynamics simulations and free-energy calculation techniques, complemented with isothermal titration calorimetry, provided insight into the binding between RB and a collagen-like peptide (CLP) at the atomic level. Electrostatic interactions dominated, which is consistent with the finding that RB bound equally well to triple helical and single chain collagen. The binding free energy ranged from -5.7 to -3 kcal/mol and was strongest near the positively charged amino groups at the N-terminus and on lysine side chains. At high RB concentration, a maximum of 16 +/- 3 bound dye molecules per peptide was found, which is consistent with spectroscopic evidence for aggregated RB bound to collagen or the CLP. Within a tissue-mimetic collagen matrix, RB photobleached rapidly, probably due to electron transfer to certain protein amino acids, as was demonstrated in solutions of free RB and arginine. In the presence of arginine and low oxygen concentrations, a product absorbing at 510 nm formed, presumably due to dehalogenation after electron transfer to RB. In the collagen matrix without arginine, the dye generated singlet oxygen as well as the 510 nm product. These results provide the first evidence of the effects of a tissue-like environment on the photochemical mechanisms of rose Bengal. | - |
dc.language | English | - |
dc.publisher | AMER CHEMICAL SOC | - |
dc.title | Rose Bengal Binding to Collagen and Tissue Photobonding | - |
dc.type | Article | - |
dc.identifier.wosid | 000418744000039 | - |
dc.identifier.scopusid | 2-s2.0-85032695422 | - |
dc.type.rims | ART | - |
dc.citation.volume | 2 | - |
dc.citation.issue | 10 | - |
dc.citation.beginningpage | 6646 | - |
dc.citation.endingpage | 6657 | - |
dc.citation.publicationname | ACS OMEGA | - |
dc.identifier.doi | 10.1021/acsomega.7b00675 | - |
dc.contributor.localauthor | Roh, HeeGwang | - |
dc.contributor.nonIdAuthor | Alarcon, Emilio I. | - |
dc.contributor.nonIdAuthor | Poblete, Horacio | - |
dc.contributor.nonIdAuthor | Couture, Jean-Francois | - |
dc.contributor.nonIdAuthor | Comer, Jeffrey | - |
dc.contributor.nonIdAuthor | Kochevar, Irene E. | - |
dc.description.isOpenAccess | Y | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | GENERAL FORCE-FIELD | - |
dc.subject.keywordPlus | MOLECULAR-DYNAMICS | - |
dc.subject.keywordPlus | CROSS-LINKING | - |
dc.subject.keywordPlus | SINGLET OXYGEN | - |
dc.subject.keywordPlus | XANTHENE DYES | - |
dc.subject.keywordPlus | GREEN LIGHT | - |
dc.subject.keywordPlus | AGGREGATION | - |
dc.subject.keywordPlus | REPAIR | - |
dc.subject.keywordPlus | MODEL | - |
dc.subject.keywordPlus | WATER | - |
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