The molecular mechanism of photoporphyrin (YHPD)'s photosensitization--laser Raman spectroscopic study of microcosmic and photosensitive damage of YHPD to protein.

Abstract

Laser Raman spectroscopy was used to investigate the microcosmic and photosensitive damage of YHPD to lysozyme, of which the three-dimensional structure has been elucidated. The experimental results shown by various damages of the main-chain and side-chain of lysozyme are as follows: (i) Phe and Cys are also damaged by photosensitization of YHPD, except for Trp, Tyr, Met, 1/2Cys and His; (ii) the order of the photosensitized sensitivity of various groups of these amino acids have been described; (iii) Trp and Tyr buried in the three-dimensional structure of the protein are damaged very greatly, and (iv) the main-chain conformation of the protein has changed considerably, such as a decrease in orderly structure (alpha-helix, beta-sheet and beta-turn) and a simultaneous increase in random

• Authors: Z Y Zhang, Y M Xu
• Journal: Science in China. Series B, Chemistry, life sciences & earth sciences (Sci China B) Vol. 35 Issue 4 Pg. 437-44 (Apr 1992) ISSN: 1001-652X [Print] China
• PMID: 1534229 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Hematoporphyrins
• Radiation-Sensitizing Agents
• Hematoporphyrin Derivative
• Muramidase

Topics

• Hematoporphyrin Derivative
• Hematoporphyrins (pharmacology)
• Molecular Conformation
• Muramidase (drug effects)
• Radiation-Sensitizing Agents (pharmacology)
• Spectrum Analysis, Raman