2012
DOI: 10.1016/j.jct.2012.01.024
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Volumetric, conductometric and fluorescence probe studies of interactions between glycyl dipeptides and sodium caprylate in aqueous media

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Cited by 8 publications
(7 citation statements)
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“…The trend can probably be regarded to larger hydrophobic/ non-polar character of the side chain of the former, which causes greater electrostriction at the terminal charged groups and hence increase in V 2;/ values. Similar results were found for amino acids and/or dipeptides in aqueous sodium carboxylate solutions [14][15][16], ionic liquid [18], methanoic acid [20], sodium fluoride [22], cetyltrimethylammonium bromide solutions [23], furosemide [10], and so on.…”
Section: Resultssupporting
confidence: 78%
See 1 more Smart Citation
“…The trend can probably be regarded to larger hydrophobic/ non-polar character of the side chain of the former, which causes greater electrostriction at the terminal charged groups and hence increase in V 2;/ values. Similar results were found for amino acids and/or dipeptides in aqueous sodium carboxylate solutions [14][15][16], ionic liquid [18], methanoic acid [20], sodium fluoride [22], cetyltrimethylammonium bromide solutions [23], furosemide [10], and so on.…”
Section: Resultssupporting
confidence: 78%
“…The systematic study of DB-small biomolecule interactions can provide valuable information about small biomolecules' behavior and insight into the conformational stability of proteins in antibacterial drug DB solutions. Taking these into consideration and in continuation to our work on thermodynamics studies [14][15][16][17], in this present paper we report the volumetric properties of simple a-amino acids like glycine, L-alanine, L-valine, L-leucine and three glycyl dipeptides glycylglycine, glycyl-L-valine and glycyl-L-leucine in aqueous domiphen bromide (DB) solutions at different temperatures. The temperature range in our study (293.…”
Section: Introductionmentioning
confidence: 92%
“…The relatively freer NH 3 + and COO − end Table 1 Standard partial molar volumes (V 2,φ 0 ) and experimental slopes S V for three glycyl dipeptides in aqueous [C n mim]Br (n=10, 14) solutions at different temperatures groups in glycylglycine will cause the maximum volume contraction followed by glycylvaline and least by glycylleucine in which the polar end groups are highly shielded by the bulky group -CHCH 3 CH 3 for electrostriction. Similar results were found for dipeptides in aqueous sodium carboxylate solutions [18][19][20][21] and amino acid in aqueous ionic liquid [5,22], methanoic acid [23], sodium fluoride [24], cetyltrimethylammonium bromide solutions [25], and so on. Furthermore, Fig.…”
Section: Resultssupporting
confidence: 78%
“…For an amphiphillic molecule such as an alcohol, with both hydrophilic and hydrophobic groups it is known that the cosphere on the −OH group of alcohol is considerably different from the cosphere on −CH 2 − or CH 3 (of the alkyl chain), which are more or less similar to each other. 32 It is reported 33 that the overlap of cospheres of two ionic groups leads to an increase in volume, whereas the overlap of cospheres of hydrophobic groups with that of either ionic or hydrophobic groups results in a net decrease in volume. Kumar et al 29 also observed a similar variation of V φ with bile salt concentration in aqueous amino acid solutions which has been related to the dominance of electrostatic interactions between bile salts and amino acids at lower surfactant (bile salt) concentrations followed by the dominating hydrophobic interactions at higher surfactant concentrations.…”
Section: Resultsmentioning
confidence: 99%