Differential interactions and structural stability of chitosan oligomers with human serum albumin and α-1-glycoprotein

Gokara, Mahesh ; Kimavath, Geetha Bai ; Podile, Appa Rao ; Subramanyam, Rajagopal (2015) Differential interactions and structural stability of chitosan oligomers with human serum albumin and α-1-glycoprotein Journal of Biomolecular Structure and Dynamics, 33 (1). pp. 196-210. ISSN 0739-1102

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Official URL: http://www.tandfonline.com/doi/full/10.1080/073911...

Related URL: http://dx.doi.org/10.1080/07391102.2013.868321


Chitosan is a naturally occurring deacetylated derivative of chitin with versatile biological activities. Here, we studied the interaction of chitosan oligomers with low degree of polymerization such as chitosan monomer (CM), chitosan dimer (CD), and chitosan trimer (CT) with human serum albumin (HSA) a major blood carrier protein and α-1-glycoprotein (AGP). Since, HSA and AGP are the two important plasma proteins that determine the drug disposition and affect the fate of distribution of drugs. Fluorescence emission spectra indicated that CM, CD, and CT had binding constants of KCM = 6.2 ± .01 × 105 M−1, KCD = 5.0 ± .01 × 104 M−1, and KCT = 1.6 ± .01 × 106 M−1, respectively, suggesting strong binding with HSA. However, binding of chitooligomers with AGP was insignificant. Thermodynamic and molecular docking analysis indicated that hydrogen bonds and also hydrophobic interaction played an important role in stabilizing the HSA-chitooligomer complexes with free energies of −7.87, −6.35, and −8.4 Kcal/mol for CM, CD, and CT, respectively. Further, circular dichroism studies indicated a minor unfolding of HSA secondary structure, upon interaction with chitooligomers, which are supported with fluctuations of root mean square deviation (RMSD) and radius of gyration (Rg) of HSA. Docking analysis revealed that all three chitooligomers were bound to HSA within subdomain IIA (Site I). In addition, RMSD and Rg analysis depicted that HSA-chitooligomer complexes stabilized at around 4.5 ns. These results suggest that HSA might serve as a carrier in delivering chitooligomers to target tissues than AGP which has pharmacological importance.

Item Type:Article
Source:Copyright of this article belongs to Taylor & Francis.
Keywords:Chitooligomers; Drug Binding; Fluorescence Quenching; α-Glycoprotein; Human Serum Albumin; Molecular Dynamics Simulation
ID Code:103942
Deposited On:09 Mar 2018 10:56
Last Modified:09 Mar 2018 10:56

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