PubMed · 1838770
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J D Spikes. 1991. What does HPD really mean?. https://doi.org/10.1016/1011-1344(91)80023-b
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The effects of pH on the binding of hematoporphyrin derivative (HpD) to monolayer and bilayer membranes have been studied. Absorption spectra of HpD bound to phosphatidylcholine (PC) liposomes indicate that there is greater binding of HpD to lipid films at acidic, tumoricidal pH conditions than at normal tissue pH. These results were found to correlate with surface pressure measurements of monolayer films formed under similar conditions. Surface potential measurements in conjunction with surface pressure measurements from monolayer films suggest that at low pH (i.e. less than or equal to 6.6) porphyrin intercalates within the lipid film to reach relatively high concentrations, while at higher pH (i.e. greater than or equal to 7.4) the porphyrin preferably adsorbs to the lipid film at the monolayer/water interface.
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