Interaction of Silver Nanoparticles with Human Alpha-2-macroglobulin: Biochemical and Biophysical Investigation
Abstract
Background: Silver nanoparticles (AgNPs) have a broad spectrum of applications in nanoscience and nanomedicine due to their flexible properties, such as antibacterial, antifungal, anti-inflammatory and anti-angiogenic. Present study investigated the interaction of chemically synthesized AgNPs with human major antiproteinase alpha-2-macroglobulin (α2M).
Materials and methods: The first step of the study involved the synthesis and characterization of AgNPs using various biochemical and biophysical techniques, such as UV-visible spectroscopy, fluorescence quenching spectroscopy, synchronous fluorescence, and circular dichroism (CD). Different methods were used to explore the primary and secondary structural changes induced in α2M by the binding of AgNPs.
Results: The UV-visible spectroscopy revealed hyperchromicity in the absorption spectra of α2M. The presence of a static quenching mechanism was indicated by the temperature-dependent fluorescence spectroscopy. The synchronous fluorescence revealed a change in the microenvironment of the tryptophan residues in α2M. The CD results showed the reduction in β-helical content of α2M. The activity of α2M decreased significantly with the increase of AgNPs concentration.
Conclusion: Our result suggests that AgNPs cause modifications in the structure and functional activity of α2M. The interaction of nanoparticles with proteins is important for understanding their potential risks to human health.
Keywords: alpha-2-macroglobulin, antiproteinase, silver nanoparticles, fluorescence quenching, FTIR, TEM
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Gnanadhas DP, Ben Thomas M, Thomas R, Raichur AM, Chakravortty D. Interaction of silver nanoparticles with serum proteins affects their antimicrobial activity in vivo. Antimicrob Agents Chemother. 2013; 57(10): 4945-55, CrossRef.
Meng H, Liong M, Xia T, Li Z, Ji Z, Zink JI, et al. Engineered design of mesoporous silica nanoparticles to deliver doxorubicin and P-glycoprotein siRNA to overcome drug resistance in a cancer cell line. ACS Nano. 2010; 4(8): 4539-50, CrossRef.
Kohl Y, Kaiser C, Bost W, Stracke F, Fournelle M, Wischke C, et al. Preparation and biological evaluation of multifunctional PLGA-nanoparticles designed for photoacoustic imaging. Nanomedicine. 2011; 7(2): 228-37, CrossRef.
Saptarshi SR, Duschl A, Lopata AL. Interaction of nanoparticles with proteins: Relation to bio-reactivity of the nanoparticle. J Nanobiotechnology. 2013; 11: 26, CrossRef.
Dasgupta N, Ranjan S, Patra D, Srivastava P, Kumar A, Ramalingam C. Bovine serum albumin interacts with silver nanoparticles with a “side-on” or “end on” conformation, Chem-Biol Interact. 2016; 253: 100-11, CrossRef.
Zhang XF, Liu ZG, Shen W, Gurunathan S. Silver nanoparticles: Synthesis, characterization, properties, applications, and therapeutic approaches. Int J Mol Sci. 2016; 17(9): 1534, CrossRef.
Mishra M, Kumar H, Tripathi K. Diabetic delayed wound healing and the role of silver nanoparticles. Dig J Nanomater Biostructures. 2008; 3(2): 109-13, article.
Iranfar H, Rajabi O, Salari R, Chamani J. Probing the interaction of human serum albumin with ciprofloxacin in the presence of silver nanoparticles of three sizes: Multispectroscopic and ζ potential investigation. J Phys Chem B. 2012; 116(6): 1951-64, CrossRef.
Siddiqui T, Zia MK, Ali SS, Rehman AA, Ahsan H, Khan FH. Reactive oxygen species and anti-proteinases. Arch Physiol Biochem. 2016; 122(1): 1-7, CrossRef.
Kaur I, Katyal A. Modification of mouse A2M B (620-792) and A2M N (168-230) by malondialdehyde and acetaldehyde attenuates the proteinase and TGF-β1 binding ability of A2MB. FEBS Lett. 2011; 585(6): 829-33, CrossRef.
Rehman AA, Ahsan H, Khan FH. α-2-Macroglobulin: a physiological guardian. J Cell Physiol. 2013; 228(8): 1665-75, CrossRef.
Rabbani G, Khan MJ, Ahmad A, Maskat MY, Khan RH. Effect of copper oxide nanoparticles on the conformation and activity of β-galactosidase. Colloids Surf B Biointerfaces. 2014; 123: 96-105, CrossRef.
Iravani S, Korbekandi H, Mirmohammadi SV, Zolfaghari B. Synthesis of silver nanoparticles: Chemical, physical and biological methods. Res Pharm Sci. 2014; 9(6): 385-406, article.
Khatoon UT, Rao KV, Ramana Rao JV, Aparna Y. Synthesis and characterization of silver nanoparticles by chemical reduction method. In: Jeppiaar J, Chetal SSC, editors. International Conference on Nanoscience, Engineering and Technology 2011 Nov 28-30, Chennai. Manhattan: IEEE; 2011. p. 97-9, CrossRef.
Wiley B, Sun Y, Mayers B, Xia Y. Shape-controlled synthesis of metal nanostructures: The case of silver. Chemistry. 2005; 11(2): 454-63, CrossRef.
Evanoff DD, Chumanov G. Size-controlled synthesis of nanoparticles. 2. measurement of extinction, scattering, and absorption cross sections, J Phys Chem B. 2004; 108(37): 13957–62, CrossRef.
Oliveira MM, Ugarte D, Zanchet D, Zarbin AJ. Influence of synthetic parameters on the size, structure, and stability of dodecanethiol-stabilized silver nanoparticles. J Colloid Interface Sci. 2005; 292(2): 429-35, CrossRef.
He Y, Wei F, Ma Z, Zhang H, Yang Q, Yao B, et al. Green synthesis of silver nanoparticles using seed extract of Alpinia katsumadai, and their antioxidant, cytotoxicity, and antibacterial activities. RSC Adv. 2017; 7: 39842-51, CrossRef.
Zia MK, Siddiqui T, Ali SS, Ahsan H, Khan FH. Interaction of anti-cancer drug-cisplatin with major proteinase inhibitor-alpha-2-macroglobulin: Biophysical and thermodynamic analysis. Int J Biol Macromol. 2018; 116: 721-7, CrossRef.
Zia MK, Siddiqui T, Ahsan H, Khan FH. Comprehensive insight into the molecular interaction of an anticancer drug-ifosfamide with human alpha-2-macroglobulin: Biophysical and in silico studies. J Biomol Struct Dyn. 2022; 40(9): 3907-16, CrossRef.
Zia MK, Siddiqui T, Ali SS, Ahsan H, Khan FH. Deciphering the binding of dutasteride with human alpha-2-macroglobulin: Molecular docking and calorimetric approach. Int J Biol Macromol. 2019; 133: 1081-9, CrossRef.
Zia MK, Siddiqui T, Ahsan H, Khan FH. Characterization of the binding between anti-tumor drug 5-fluorouracil and human alpha-2-macroglobulin: Spectroscopic and molecular docking analyses. J Biomol Struct Dyn. 2021; ahead of print: 1-11, CrossRef.
Siddiqui T, Zia MK, Ali SS, Ahsan H, Khan FH. Inactivation of alpha-2-macroglobulin by photo-illuminated gallic acid. J Fluoresc. 2019; 29(4): 969-79, CrossRef.
Siddiqui T, Zia MK, Ali SS, Ahsan H, Khan FH. Investigating hydrogen peroxide induced damage to alpha-2-macroglobulin: Biophysical and thermodynamic study. J Mol Struct. 2019; 1195: 904-13, CrossRef.
Siddiqui T, Zia MK, Ali SS, Ahsan H, Khan FH. Insight into the interactions of proteinase inhibitor- alpha-2-macroglobulin with hypochlorite. Int J Biol Macromol. 2018; 117: 401-6, CrossRef.
Siddiqui T, Zia MK, Ahsan H, Khan FH. Quercetin-induced inactivation and conformational alterations of alpha-2-macroglobulin: Multi-spectroscopic and calorimetric study. J Biomol Struct Dyn. 2020; 38(14): 4107-18, CrossRef.
Kumar B, Smita K, Seqqat R, Benalcazar K, Grijalva M, Cumbal L. In vitro evaluation of silver nanoparticles cytotoxicity on Hepatic cancer (Hep-G2) cell line and their antioxidant activity: Green approach for fabrication and application. J Photochem Photobiol B. 2016; 159: 8-13, CrossRef.
Shukla VK, Yadav RS, Yadav P, Pandey AC. Green synthesis of nanosilver as a sensor for detection of hydrogen peroxide in water. J Hazard Mater. 2012; 213-214: 161-6, CrossRef.
Zia MK, Siddiqui T, Ali SS, Ahsan H, Khan FH. Understanding the binding interaction between methotrexate and human alpha-2-macroglobulin: Multi-spectroscopic and computational investigation. Arch Biochem Biophys. 2019; 675: 108118, CrossRef.
Zia MK, Siddiqui T, Ali SS, Ahsan H, Khan FH. Exploring the interaction of anti-androgen drug-bicalutamide with human alpha-2-macroglobulin: A biophysical investigation. Int J Biol Macromol. 2018; 120(Pt B): 2285-92, CrossRef.
Banerjee V, Das KP. Interaction of silver nanoparticles with proteins: A characteristic protein concentration dependent profile of SPR signal. Colloids Surf B Biointerfaces. 2013; 111: 71-9, CrossRef.
Hu YJ, Liu Y, Wang JB, Xiao XH, Qu SS. Study of the interaction between monoammonium glycyrrhizinate and bovine serum albumin. J Pharm Biomed Anal. 2004; 36(4): 915-9, CrossRef.
Anand U, Jash C, Boddepalli RK, Shrivastava A, Mukherjee S. Exploring the mechanism of fluorescence quenching in proteins induced by tetracycline. J Phys Chem B. 2011; 115(19): 6312-20, CrossRef.
Mariam J, Dongre PM, Kothari DC. Study of interaction of silver nanoparticles with bovine serum albumin using fluorescence spectroscopy. J Fluoresc. 2011; 21(6): 2193-9, CrossRef.
Roy S, Das TK. Spectroscopic studies of interaction between biologically synthesized silver nanoparticles and bovine serum albumin. J Nanosci Nanotechnol. 2014; 14(7): 4899-905, CrossRef.
Perez-Iratxeta C, Andrade-Navarro MA. K2D2: Estimation of protein secondary structure from circular dichroism spectra. BMC Struct Biol. 2008; 8: 25, CrossRef.
Zia MK, Siddiqui T, Ali SS, Rehman AA, Ahsan H, Khan FH. Chemotherapeutic drugs and plasma proteins: Exploring new dimensions. Curr Protein Pept Sci. 2018; 19(10): 937-47, CrossRef.
Ali SS, Ahsan H, Ansari S, Abdullah KM, Khan FH. Photo-illuminated glutathione inactivates alpha-2-macroglobulin: Spectroscopic and thermodynamic studies. Mol Cell Biomed Sci. 2022; 6(1): 35-42, CrossRef.
DOI: https://doi.org/10.21705/mcbs.v6i3.281
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