title: Multi-spectroscopic and molecular modeling studies of interaction between two different angiotensin I converting enzyme inhibitory peptides from gluten hydrolysate and human serum albumin.
abstract: The present study was carried out to characterize Angiotensin-converting enzyme (ACE) inhibitory peptides which are released from the trypsin hydrolysate of wheat gluten protein. The binding of two inhibitory peptide (P4and P6) to human serum albumin (HSA) under physiological conditions has been investigated by multi-spectroscopic in combination with molecular modeling techniques. Time-resolved and quenching fluorescence spectroscopies results revealed that the quenching of HSA fluorescence by P4and P6in the binary and ternary systems caused HSA-peptides complexes formation. The results indicated that both peptides quenched the fluorescence intensity of HSA through a static mechanism. The binding affinities and number of binding sites were obtained for the HSA-peptides complexes. The circular dichroism (CD) data revealed that the presence of both peptides increased the α-helix content of HSA and induced the remarkable folding of the polypeptide of the protein. Therefore, the CD data determined that the protein structure has been stabilized in the percent of ACE inhibitory peptides in binary and ternary systems. The binding distances between HSA and both peptides were estimated by the Forster theory, and it was revealed that nonradiative energy transfer from HSA to peptides occurred with a high probability. ITC experiments reveal that, in the absence and presence of P6, the dominant forces are electrostatic in binary and ternary systems. Furthermore, molecular modeling studies confirmed the experimental results. Molecular modeling investigation suggested that P4bound to the site IA and IIA of HSA in binary and ternary systems, respectively. This study on the interaction of peptides with HSA should prove helpful for realizing the distribution and transportation of food compliments and drugs in vivo, elucidating the action mechanism and dynamics of food compliments and drugs at the molecular level. It should moreover be of great use for understanding the pharmacokinetic and pharmacodynamic mechanism of the food compliments and drugs.
authors.affiliation: a Department of Biology, Faculty of Science , University of Shahrekord , P.O. Box 115 , Shahrekord , Iran.
authors.forename: Reza
authors.initials: R
authors.lastname: Assaran Darban
authors.affiliation: a Department of Biology, Faculty of Science , University of Shahrekord , P.O. Box 115 , Shahrekord , Iran.
authors.forename: Behzad
authors.initials: B
authors.lastname: Shareghi
authors.affiliation: b Department of Chemistry, Faculty of Sciences , Ferdowsi University of Mashhad , Mashhad , Iran.
authors.forename: Ahmad
authors.initials: A
authors.lastname: Asoodeh
authors.affiliation: c Department of Biochemistry and Biophysics, Faculty of Sciences , Mashhad Branch, Islamic Azad University , Mashhad , Iran.
authors.forename: Jamshidkhan
authors.initials: J
authors.lastname: Chamani
mesh_terms: D020816:Amino Acid Motifs; D000806:Angiotensin-Converting Enzyme Inhibitors / Q000737:chemistry* / Q000302:isolation & purification; D001665:Binding Sites; D005983:Glutens / Q000737:chemistry* / Q000302:isolation & purification; D006801:Humans; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D007700:Kinetics; D062105:Molecular Docking Simulation; D056004:Molecular Dynamics Simulation; D007703:Peptidyl-Dipeptidase A / Q000737:chemistry*; D011485:Protein Binding; D011492:Protein Hydrolysates / Q000737:chemistry* / Q000302:isolation & purification; D054730:Protein Interaction Domains and Motifs; D017433:Protein Structure, Secondary; D000075462:Serum Albumin, Human / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D055672:Static Electricity; D013816:Thermodynamics
chemical_list: D000806:Angiotensin-Converting Enzyme Inhibitors; D011492:Protein Hydrolysates; D005983:Glutens; C488034:ACE protein, human; D007703:Peptidyl-Dipeptidase A; D000075462:Serum Albumin, Human
keywords: ACE inhibitory peptides; fluorescence spectroscopy; human serum albumin; molecular modeling