2016
DOI: 10.1016/j.jct.2016.06.018
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Intermolecular interactions of α-amino acids and glycyl dipeptides with the drug domiphen bromide in aqueous solutions analyzed by volumetric and UV–vis spectroscopy methods

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Cited by 32 publications
(4 citation statements)
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“…Grape seed protein has a strong absorption peak at 200 nm and a weak absorption peak at 277 nm, while GSPP has a strong absorption peak at 212 nm and a weak absorption peak at 277 nm. This may be due to the transition of C=O from π‐π * and the phenylalanine colour transition in peptide bonds (Yan et al ., 2016). After reacting with calcium ions, GSP‐Ca shows only one absorption peak with the decreased intensity, and the peak position shifted from 200 to 196 nm, indicating a blue shift.…”
Section: Resultsmentioning
confidence: 99%
“…Grape seed protein has a strong absorption peak at 200 nm and a weak absorption peak at 277 nm, while GSPP has a strong absorption peak at 212 nm and a weak absorption peak at 277 nm. This may be due to the transition of C=O from π‐π * and the phenylalanine colour transition in peptide bonds (Yan et al ., 2016). After reacting with calcium ions, GSP‐Ca shows only one absorption peak with the decreased intensity, and the peak position shifted from 200 to 196 nm, indicating a blue shift.…”
Section: Resultsmentioning
confidence: 99%
“…The peanut peptide showed significant absorptions at 207 and 279 nm (Z. Yan et al, 2016). After chelation with zinc, the absorption peaks moved to 205 and 274 nm, respectively, with that at 274 nm decreased significantly.…”
Section: Uv Spectroscopymentioning
confidence: 98%
“…2−5 Moreover, different types of interactions between amino acids and their surroundings impact the conformational stability of proteins as well. 6−9 Physicochemical investigations of amino acids 10−17 or short peptides 18,19 in water are crucial to understanding the different interactions and structural transmutations of amino acids/proteins. Ionic liquids' (ILs) nonvolatile characteristics at room temperature make them the most versatile additives, allowing them to be utilized with different ions in a variety of combinations.…”
Section: Introductionmentioning
confidence: 99%
“…Amino acids, considered as the building blocks of proteins, are made up of carboxyl, amino functional groups, and side chain(s). The addition or removal of alkyl groups or any other substituent in the side chain drastically alters the thermophysical characteristics of amino acids. Moreover, different types of interactions between amino acids and their surroundings impact the conformational stability of proteins as well. Physicochemical investigations of amino acids or short peptides , in water are crucial to understanding the different interactions and structural transmutations of amino acids/proteins.…”
Section: Introductionmentioning
confidence: 99%