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Article Open Access September 04, 2022

Drug-Receptor Interaction of Peptidic HIV-1 Protease: The Hydrophobic Effect-I

Vishnu Kumar Sahu 1,*, Rajesh Kumar Singh 1 and Pashupati Prasad Singh 1
1
Department of Chemistry, Maharani Lal Kunwari Post Graduate College, Balrampur, U.P.271201, India
Publihed in: Current Research in Public Health (Volume 1, Issue 1, 2022)
Page(s): 33-48
DOI: 10.31586/ojmr.2022.411
Received
July 21, 2022
Revised
August 25, 2022
Accepted
September 02, 2022
Published
September 04, 2022
Keywords
Hydrophobicity; Solvent Accessible Surface Area; PM3
Creative Commons

This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.
Copyright: Copyright © The Author(s), 2022. Published by Scientific Publications
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Cite This Article

APA Style
Sahu, V. K. , Singh, R. K. , & Singh, P. P. (2022). Drug-Receptor Interaction of Peptidic HIV-1 Protease: The Hydrophobic Effect-I. Current Research in Public Health, 1(1), 33-48. https://doi.org/10.31586/ojmr.2022.411
ACS Style
Sahu, V. K. ; Singh, R. K. ; Singh, P. P. Drug-Receptor Interaction of Peptidic HIV-1 Protease: The Hydrophobic Effect-I. Current Research in Public Health 2022 1(1), 33-48. https://doi.org/10.31586/ojmr.2022.411
Chicago/Turabian Style
Sahu, Vishnu Kumar, Rajesh Kumar Singh, and Pashupati Prasad Singh. 2022. "Drug-Receptor Interaction of Peptidic HIV-1 Protease: The Hydrophobic Effect-I". Current Research in Public Health 1, no. 1: 33-48. https://doi.org/10.31586/ojmr.2022.411
AMA Style
Sahu VK, Singh RK, Singh PP. Drug-Receptor Interaction of Peptidic HIV-1 Protease: The Hydrophobic Effect-I. Current Research in Public Health. 2022; 1(1):33-48. https://doi.org/10.31586/ojmr.2022.411 
@Article{crph411,
AUTHOR = {Sahu, Vishnu Kumar and Singh, Rajesh Kumar and Singh, Pashupati Prasad},
TITLE = {Drug-Receptor Interaction of Peptidic HIV-1 Protease: The Hydrophobic Effect-I},
JOURNAL = {Current Research in Public Health},
VOLUME = {1},
YEAR = {2022},
NUMBER = {1},
PAGES = {33-48},
URL = {https://www.scipublications.com/journal/index.php/OJMR/article/view/411},
ISSN = {2831-5162},
DOI = {10.31586/ojmr.2022.411},
ABSTRACT = {When a drug interacts with its receptor, the nonpolar substituent of drug and receptor proteins attract each other because they have opposite magnitude with respect to each other. X-rays structure studies reflected that the S2/S2’ pocket in HIV-1 protease enzyme are essentially hydrophobic. The residues that make up these pockets are Val-32, Ile-47, Ile-50, and Ile-84 in each monomeric polypeptidic unit of the protease enzyme. Δπdr and ΔSASAdr have been used to measure the extent of hydrophobic interaction between peptidic protease inhibitors and receptor proteins (binding site: valine‒isoleucine; and catalytic site: glycine‒aspartic acid‒threonine) on the HIV-1 protease enzyme. For measurement of hydrophobic interaction, the molecular modeling and geometry optimization of all the inhibitors and the receptor amino acids have been carried out with CAChe Pro software by opting semiempirical PM3 methods. Log P was calculated using the atom-typing scheme of Ghose and Crippen, while solvent accessible surface area by conductor likes screening model. πd, πr, SASASd and SASASr well describe the hydrophobicities of the substituents and play the effective role for site selectivity for interaction of the drug with the receptor. Comparative study of values of Δπdr and ΔSASAdr show the order of hydrophobic interaction with respect to amino acids: Asp > Thr > Val > Ile and Thr > Val > Asp > Ile, respectively. Further, comparative study of the values of (ΣΔπdr)binding-site, (ΣΔπdr)catalytic-site, (ΣΔSASAdr)binding-site, (ΣΔSASAdr)catalytic-site shows that peptidic HIV-1-PRIs interact with binding site rather than catalytic site as binding site have lower value of ΣΔπdr and ΣΔSASAdr. Among the binding site, Val has maximum interaction than Ile, as it has lower vale of Δπdr and ΔSASAdr.},
}
%0 Journal Article
%A Sahu, Vishnu Kumar
%A Singh, Rajesh Kumar
%A Singh, Pashupati Prasad
%D 2022
%J Current Research in Public Health

%@ 2831-5162
%V 1
%N 1
%P 33-48

%T Drug-Receptor Interaction of Peptidic HIV-1 Protease: The Hydrophobic Effect-I
%M doi:10.31586/ojmr.2022.411
%U https://www.scipublications.com/journal/index.php/OJMR/article/view/411

TY  - JOUR
AU  - Sahu, Vishnu Kumar
AU  - Singh, Rajesh Kumar
AU  - Singh, Pashupati Prasad
TI  - Drug-Receptor Interaction of Peptidic HIV-1 Protease: The Hydrophobic Effect-I
T2  - Current Research in Public Health
PY  - 2022
VL  - 1
IS  - 1
SN  - 2831-5162
SP  - 33
EP  - 48
UR  - https://www.scipublications.com/journal/index.php/OJMR/article/view/411
AB  - When a drug interacts with its receptor, the nonpolar substituent of drug and receptor proteins attract each other because they have opposite magnitude with respect to each other. X-rays structure studies reflected that the S2/S2’ pocket in HIV-1 protease enzyme are essentially hydrophobic. The residues that make up these pockets are Val-32, Ile-47, Ile-50, and Ile-84 in each monomeric polypeptidic unit of the protease enzyme. Δπdr and ΔSASAdr have been used to measure the extent of hydrophobic interaction between peptidic protease inhibitors and receptor proteins (binding site: valine‒isoleucine; and catalytic site: glycine‒aspartic acid‒threonine) on the HIV-1 protease enzyme. For measurement of hydrophobic interaction, the molecular modeling and geometry optimization of all the inhibitors and the receptor amino acids have been carried out with CAChe Pro software by opting semiempirical PM3 methods. Log P was calculated using the atom-typing scheme of Ghose and Crippen, while solvent accessible surface area by conductor likes screening model. πd, πr, SASASd and SASASr well describe the hydrophobicities of the substituents and play the effective role for site selectivity for interaction of the drug with the receptor. Comparative study of values of Δπdr and ΔSASAdr show the order of hydrophobic interaction with respect to amino acids: Asp > Thr > Val > Ile and Thr > Val > Asp > Ile, respectively. Further, comparative study of the values of (ΣΔπdr)binding-site, (ΣΔπdr)catalytic-site, (ΣΔSASAdr)binding-site, (ΣΔSASAdr)catalytic-site shows that peptidic HIV-1-PRIs interact with binding site rather than catalytic site as binding site have lower value of ΣΔπdr and ΣΔSASAdr. Among the binding site, Val has maximum interaction than Ile, as it has lower vale of Δπdr and ΔSASAdr.
DO  - Drug-Receptor Interaction of Peptidic HIV-1 Protease: The Hydrophobic Effect-I
TI  - 10.31586/ojmr.2022.411
ER  -