Molecular docking analysis of subtilisin-like alkaline serine protease (SLASP) and laccase with natural biopolymers

• Published in: Open Chemistry Vol. 22; no. 1
• Main Authors: Narayanaswamy, Radhakrishnan, Prabhakaran, Vasantha-Srinivasan, Al-Otibi, Fatimah Oleyan, Alharbi, Raedah Ibrahim, Ibrahim, Kalibulla Syed
• Format: Journal Article
• Language: English
• Published: De Gruyter 30.09.2024
• Subjects: chitosan; laccase; MD simulation; molecular docking; nanoparticles; natural biopolymer; subtilisin-like alkaline serine protease
• ISSN: 2391-5420; 2391-5420
• DOI: 10.1515/chem-2024-0090

Alkaline serine proteases (ASPs) and laccases (Lacs) have been reported to possess several industrial applications, particularly in the food, cosmetic, and leather industries. Thus, in the present study, eighteen natural biopolymers, including agar, agarose, alginate, kappa carrageenan, cellulose, chitosan pentamer, chitosan oligosaccharide, chondroitin sulfate, dextran, fucoidan, heparin, hyaluronan, lignin, mannan, pectin, phytic acid, pullulan and starch soluble, were studied for their docking behavior, such as subtilisin-like alkaline serine protease (SLASP) KP-43 and laccase (Bs Lac), using the SwissDock method. Additionally, the toxicity toward honey bees and human liver was determined by utilizing the free Bee-Tox and pkCSM web servers, respectively. Bee-Tox analysis demonstrated that four ligands (namely, agar, cellulose, lignin, and pullulan) exhibited acute oral toxicity toward honey bees ( ). The docking study revealed that chitosan pentamer and lignin exhibited maximum binding energies of −9.67 and −11.37 kcal/mol against the target proteins SLASP (KP-43) and Lac (Bs Lac), respectively. Interestingly, in the present study, agarose was shown to interact with the His68 and Ser255 amino acid residues of SLASP (KP-43) from KSM-KP43 sp. Thus, the current investigation showed the potential of eighteen natural biopolymers as immobilizing agents to prepare ASP and Lac nanoparticles for biomedical applications.