A theoretical elucidation of glucose interaction with HSA's domains

Rasoul Nasiri, Homayoon Bahrami, Mansour Zahedi, Ali Akbar Moosavi-Movahedi, Naghmeh Sattarahmady

Research output: Contribution to journalArticle

Abstract

The interaction of different domains belonging to Human Serum Albumin (HSA) with open form of glucose have been investigated using molecular dynamics simulation methods. Applying docking, primary structures involving interaction of some residues with glucose have been obtained. Subsequently, equilibrium geometries at 300 K and minimum geometries have been determined for each of aforementioned structures by employing MD simulation and simulated annealing. The stability of species has been evaluated using a SAWSA v2.0 model. Ultimately, NBO analysis has been carried out to specify possible hydrogen bonding regarding the HSA interaction with glucose. Results obtained show that glucose can interact with Lys195, Lys199, and Glu153. In these interactions, each lysine forms an H-bonding with glucose. The H-bonding is obtained by stretching of N-H bond belonging to NH3 + group of lysine along an oxygen atom of glucose. In addition, the above mentioned lysines are protonated, and there is an electrostatic interaction between glucose with Lys195 or Lys199. In addition, an H-bonding is formed between O atom of –COO group belonging to Glu153 and H atom of OH group belonging to glucose. Because, the N-H group of Lys195 interacts with the O atom of latter OH group, reaction of Lys195 is more desirable than that of Lys199. In fact, glucose is placed in the vicinity of Lys195 along with electrostatic interaction and H-bonding to Lys195 and Lys199 as well as H-bonding with Glu153, which subsequently reacts with Lys195. Thus, Lys195 is the primary site in reaction of glucose with HSA.
Original languageEnglish
Pages (from-to)211-226
Number of pages16
JournalJournal of Biomolecular Structure & Dynamics
Volume28
Issue number2
DOIs
Publication statusPublished - 15 Oct 2010

Fingerprint

Glucose
Serum Albumin
Lysine
Atoms
Coulomb interactions
Geometry
Simulated annealing
Stretching
Molecular dynamics
Hydrogen bonds
Oxygen
Computer simulation

Bibliographical note

© 2010 Taylor Francis / Adenine Press

Keywords

  • Human Serum Albumin
  • Glucose
  • Molecular Dynamics Simulation
  • Simulated annealing
  • NBO Analysis

Cite this

Nasiri, R., Bahrami, H., Zahedi, M., Moosavi-Movahedi, A. A., & Sattarahmady, N. (2010). A theoretical elucidation of glucose interaction with HSA's domains. Journal of Biomolecular Structure & Dynamics, 28(2), 211-226. https://doi.org/10.1080/07391102.2010.10507354
Nasiri, Rasoul ; Bahrami, Homayoon ; Zahedi, Mansour ; Moosavi-Movahedi, Ali Akbar ; Sattarahmady, Naghmeh. / A theoretical elucidation of glucose interaction with HSA's domains. In: Journal of Biomolecular Structure & Dynamics. 2010 ; Vol. 28, No. 2. pp. 211-226.
@article{412a36174c90489da69bbbc77ceacb7a,
title = "A theoretical elucidation of glucose interaction with HSA's domains",
abstract = "The interaction of different domains belonging to Human Serum Albumin (HSA) with open form of glucose have been investigated using molecular dynamics simulation methods. Applying docking, primary structures involving interaction of some residues with glucose have been obtained. Subsequently, equilibrium geometries at 300 K and minimum geometries have been determined for each of aforementioned structures by employing MD simulation and simulated annealing. The stability of species has been evaluated using a SAWSA v2.0 model. Ultimately, NBO analysis has been carried out to specify possible hydrogen bonding regarding the HSA interaction with glucose. Results obtained show that glucose can interact with Lys195, Lys199, and Glu153. In these interactions, each lysine forms an H-bonding with glucose. The H-bonding is obtained by stretching of N-H bond belonging to NH3 + group of lysine along an oxygen atom of glucose. In addition, the above mentioned lysines are protonated, and there is an electrostatic interaction between glucose with Lys195 or Lys199. In addition, an H-bonding is formed between O atom of –COO group belonging to Glu153 and H atom of OH group belonging to glucose. Because, the N-H group of Lys195 interacts with the O atom of latter OH group, reaction of Lys195 is more desirable than that of Lys199. In fact, glucose is placed in the vicinity of Lys195 along with electrostatic interaction and H-bonding to Lys195 and Lys199 as well as H-bonding with Glu153, which subsequently reacts with Lys195. Thus, Lys195 is the primary site in reaction of glucose with HSA.",
keywords = "Human Serum Albumin, Glucose, Molecular Dynamics Simulation, Simulated annealing, NBO Analysis",
author = "Rasoul Nasiri and Homayoon Bahrami and Mansour Zahedi and Moosavi-Movahedi, {Ali Akbar} and Naghmeh Sattarahmady",
note = "{\circledC} 2010 Taylor Francis / Adenine Press",
year = "2010",
month = "10",
day = "15",
doi = "10.1080/07391102.2010.10507354",
language = "English",
volume = "28",
pages = "211--226",
journal = "Journal of Biomolecular Structure & Dynamics",
issn = "0739-1102",
number = "2",

}

Nasiri, R, Bahrami, H, Zahedi, M, Moosavi-Movahedi, AA & Sattarahmady, N 2010, 'A theoretical elucidation of glucose interaction with HSA's domains', Journal of Biomolecular Structure & Dynamics, vol. 28, no. 2, pp. 211-226. https://doi.org/10.1080/07391102.2010.10507354

A theoretical elucidation of glucose interaction with HSA's domains. / Nasiri, Rasoul; Bahrami, Homayoon; Zahedi, Mansour; Moosavi-Movahedi, Ali Akbar; Sattarahmady, Naghmeh.

In: Journal of Biomolecular Structure & Dynamics, Vol. 28, No. 2, 15.10.2010, p. 211-226.

Research output: Contribution to journalArticle

TY - JOUR

T1 - A theoretical elucidation of glucose interaction with HSA's domains

AU - Nasiri, Rasoul

AU - Bahrami, Homayoon

AU - Zahedi, Mansour

AU - Moosavi-Movahedi, Ali Akbar

AU - Sattarahmady, Naghmeh

N1 - © 2010 Taylor Francis / Adenine Press

PY - 2010/10/15

Y1 - 2010/10/15

N2 - The interaction of different domains belonging to Human Serum Albumin (HSA) with open form of glucose have been investigated using molecular dynamics simulation methods. Applying docking, primary structures involving interaction of some residues with glucose have been obtained. Subsequently, equilibrium geometries at 300 K and minimum geometries have been determined for each of aforementioned structures by employing MD simulation and simulated annealing. The stability of species has been evaluated using a SAWSA v2.0 model. Ultimately, NBO analysis has been carried out to specify possible hydrogen bonding regarding the HSA interaction with glucose. Results obtained show that glucose can interact with Lys195, Lys199, and Glu153. In these interactions, each lysine forms an H-bonding with glucose. The H-bonding is obtained by stretching of N-H bond belonging to NH3 + group of lysine along an oxygen atom of glucose. In addition, the above mentioned lysines are protonated, and there is an electrostatic interaction between glucose with Lys195 or Lys199. In addition, an H-bonding is formed between O atom of –COO group belonging to Glu153 and H atom of OH group belonging to glucose. Because, the N-H group of Lys195 interacts with the O atom of latter OH group, reaction of Lys195 is more desirable than that of Lys199. In fact, glucose is placed in the vicinity of Lys195 along with electrostatic interaction and H-bonding to Lys195 and Lys199 as well as H-bonding with Glu153, which subsequently reacts with Lys195. Thus, Lys195 is the primary site in reaction of glucose with HSA.

AB - The interaction of different domains belonging to Human Serum Albumin (HSA) with open form of glucose have been investigated using molecular dynamics simulation methods. Applying docking, primary structures involving interaction of some residues with glucose have been obtained. Subsequently, equilibrium geometries at 300 K and minimum geometries have been determined for each of aforementioned structures by employing MD simulation and simulated annealing. The stability of species has been evaluated using a SAWSA v2.0 model. Ultimately, NBO analysis has been carried out to specify possible hydrogen bonding regarding the HSA interaction with glucose. Results obtained show that glucose can interact with Lys195, Lys199, and Glu153. In these interactions, each lysine forms an H-bonding with glucose. The H-bonding is obtained by stretching of N-H bond belonging to NH3 + group of lysine along an oxygen atom of glucose. In addition, the above mentioned lysines are protonated, and there is an electrostatic interaction between glucose with Lys195 or Lys199. In addition, an H-bonding is formed between O atom of –COO group belonging to Glu153 and H atom of OH group belonging to glucose. Because, the N-H group of Lys195 interacts with the O atom of latter OH group, reaction of Lys195 is more desirable than that of Lys199. In fact, glucose is placed in the vicinity of Lys195 along with electrostatic interaction and H-bonding to Lys195 and Lys199 as well as H-bonding with Glu153, which subsequently reacts with Lys195. Thus, Lys195 is the primary site in reaction of glucose with HSA.

KW - Human Serum Albumin

KW - Glucose

KW - Molecular Dynamics Simulation

KW - Simulated annealing

KW - NBO Analysis

U2 - 10.1080/07391102.2010.10507354

DO - 10.1080/07391102.2010.10507354

M3 - Article

VL - 28

SP - 211

EP - 226

JO - Journal of Biomolecular Structure & Dynamics

JF - Journal of Biomolecular Structure & Dynamics

SN - 0739-1102

IS - 2

ER -