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Thermochemical Study of the Interaction of Cytosine and Uracil with Peptides in a Buffered Saline: Complex Formation with beta-Endorphin 30-31 (Human), L-Glutathion (Reduced) and α-L-Alanyl-L-Tyrosine.
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- Additional Information
- Source:
Publisher: MDPI Country of Publication: Switzerland NLM ID: 101092791 Publication Model: Electronic Cited Medium: Internet ISSN: 1422-0067 (Electronic) Linking ISSN: 14220067 NLM ISO Abbreviation: Int J Mol Sci Subsets: MEDLINE
- Publication Information:
Original Publication: Basel, Switzerland : MDPI, [2000-
- Subject Terms:
- Abstract:
The complex formation of uracil and cytosine with glycyl-L-glutamic acid (β-endorphin 30-31), γ-L-glutamyl-L-cysteinyl-glycine (glutathione reduced), α-L-alanyl-L-tyrosine, and α-L-alanyl-α-L-alanine in a buffered saline has been studied using dissolution calorimetry. The values of the reaction constant, the change in Gibbs energy, enthalpy, and entropy were obtained. It is shown that the ratio of the enthalpy and entropy factors depends on the charge of the peptide ion, and the number of H-bond acceptors in the peptide structure. The contributions of interaction between charged groups and polar fragments, hydrogen bonding, and stacking interaction are discussed, taking into account the effect of solvent reorganization around the reactant molecules.
- References:
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- Grant Information:
22-23-01118 Russian Science Foundation
- Contributed Indexing:
Keywords: alanyl tyrosine; beta-endorphin 30-31; cytosine; glutathion; molecular complexes; thermodynamics; uracil
- Accession Number:
3061-88-9 (alanyltyrosine)
60617-12-1 (beta-Endorphin)
42HK56048U (Tyrosine)
56HH86ZVCT (Uracil)
8J337D1HZY (Cytosine)
0 (Peptides)
GAN16C9B8O (Glutathione)
- Publication Date:
Date Created: 20230610 Date Completed: 20230612 Latest Revision: 20230612
- Publication Date:
20240829
- Accession Number:
PMC10253761
- Accession Number:
10.3390/ijms24119764
- Accession Number:
37298713
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