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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Multi-Spectroscopic and Theoretical Analysis on the Interaction between Human Serum Albumin and a Capsaicin Derivative-RPF101

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Author(s):
Chaves, Otavio Augusto [1, 2] ; Tavares, Mauricio Temotheo [3] ; Cunha, Micael Rodrigues [3] ; Parise-Filho, Roberto [3] ; Sant'Anna, Carlos Mauricio R. [1] ; Netto-Ferreira, Jose Carlos [1, 4]
Total Authors: 6
Affiliation:
[1] Univ Fed Rural Rio de Janeiro, Inst Chem, BR-465 Km 7, BR-23970000 Seropedica, RJ - Brazil
[2] SENAI Innovat Inst Green Chem, Rua Morais e Silva N 53, BR-20271030 Rio De Janeiro, RJ - Brazil
[3] Univ Sao Paulo, Dept Pharm, Prof Lineu Prestes Ave 580, Bl 13, BR-05508900 Sao Paulo, SP - Brazil
[4] Natl Inst Metrol Qual & Technol, BR-25250020 Duque De Caxias, RJ - Brazil
Total Affiliations: 4
Document type: Journal article
Source: BIOMOLECULES; v. 8, n. 3 SEP 2018.
Web of Science Citations: 3
Abstract

The interaction between the main carrier of endogenous and exogenous compounds in the human bloodstream (human serum albumin, HSA) and a potential anticancer compound (the capsaicin analogue RPF101) was investigated by spectroscopic techniques (circular dichroism, steady-state, time-resolved, and synchronous fluorescence), zeta potential, and computational method (molecular docking). Steady-state and time-resolved fluorescence experiments indicated an association in the ground state between HSA:RPF101. The interaction is moderate, spontaneous (G degrees < 0), and entropically driven (S degrees = 0.573 +/- 0.069 kJ/molK). This association does not perturb significantly the potential surface of the protein, as well as the secondary structure of the albumin and the microenvironment around tyrosine and tryptophan residues. Competitive binding studies indicated Sudlow's site I as the main protein pocket and molecular docking results suggested hydrogen bonding and hydrophobic interactions as the main binding forces. (AU)

FAPESP's process: 17/00689-0 - New antineoplastic agents: synthesis, molecular docking and antitumoral activity of capsaicinoids analogues
Grantee:Roberto Parise Filho
Support Opportunities: Regular Research Grants