Understanding of Protein Adhesion to PLGA Through Molecular Docking Analysis

Didem Mimiroğlu; Sema Zabcı

doi:10.17776/csj.1706951

Understanding of Protein Adhesion to PLGA Through Molecular Docking Analysis

Abstract

In tissue engineering, cellular adhesion is a multistep process which occurs between the cell and the specific molecules and proteins that are adsorbed from biological fluids to the material surface. Therefore, it is essential to understand the protein adsorption level and which protein can bind efficiently to the surface of the fabricated material. Although many studies in literature showing quantification of protein adsorption levels by chemical methods and some instrumental techniques, there is a notable gap in the literature regarding the application of molecular docking analysis to identify which proteins can bind effectively to material surfaces, together with the specific interactions and orientations involved. Towards this goal, the present study aimed to evaluate the interactions between FDA approved biomaterial poly(lactic-co-glycolic acid) (PLGA) surface and specific proteins which are commonly found in cell culture medium for in vitro studies, and integrins which are associated with cellular adhesion. The results showed that PLGA exhibited strong binding affinity to both BSA and integrin β2, while less stable bindings were performed by hemoglobin and 2-macroglobulin proteins. These results indicate that how molecular recognition via docking process is important for fabricating biomaterials in tissue engineering applications.

Keywords

Project Number

The Scientific and Technological Research Council of Turkey (grant no: 217M952).

Ethical Statement

Not applicable

Thanks

The authors would like to thank the Scientific and Technological Research Council of Turkey (TÜBİTAK, Grant No: 217M952) for its partial financial support.

References

[1] Berman D.I., Alfimov A.V., Zhigulskaya Z.A., Leirikh A.N., Overwintering and cold-hardiness of ants in the Northeast of Asia, Sofia-Moscow: Pensoft, (2010) 294.
[2] Berman D.I., Leirikh A.N., Bessolitzina E.P., Three strategies of cold tolerance in click beetles (Coleoptera, Elateridae), Doklady Biological Sciences, 450 (2013) 168–172.
[3] Berman D.I., Leirikh A.N., Bessolitzina E.P., Biotopical distribution and resistance to cold of click beetles (Coleoptera, Elateridae) in the Upper Kolyma basin, Euroasian Entomological Journal, (2017) 129–140.
[4] Duman J.G., The role of macromolecular antifreeze in the darkling beetle, Meracantha contracta, Journal of Comparative Physiology, (1977) 279–286.
[5] Duman J.G., Bennett V., Sformo T., Hochstrasser R., Barnes B.M., Antifreeze proteins in Alaskan insects and spiders, Journal of Insect Physiology, 50 (2004) 259–266.
[6] Duman J.G., Animal ice-binding (antifreeze) proteins and glycolipids: an over view with emphasis on physiological function, Journal of Experimental Biology, 218 (2015) 1846-1855.
[7] Storey J.M., Storey K.B., Cold hardiness and freeze tolerance, Functional Metabolism: Regulation and Adaptation, (2004).
[8] Richard E., Lee R.E. Jr., Insect Cold-Hardiness: To Freeze or Not to Freeze, BioScience, 39 (1989) 308-313.

[9] Denlinger D.L., Lee R.E. Jr., Low Temperature Biology of Insects, Cambridge University Press, (2010).
[10] Białkowska A., Majewska E., Olczak A., Twarda-Clapa A., Ice Binding Proteins: Diverse Biological Roles and Applications in Different Types of Industry, Biomolecules, 10 (2020) 274.
[11] Eastman J.T., Devries A.L., Renal glomerular evolution in Antarctic notothenioid fishes, Journal of Fish Biology, 29 (1986) 649-662.
[12] Huang T., Duman J.G., Cloning and characterization of a thermal hysteresis antifreeze protein with DNA-binding activity from winter bittersweet nightshade, Solanum dulcamara, Plant Molecular Biology, 48 (2002) 339–350.
[13] Duman J.G., Antifreeze and ice nucleator proteins in terrestrial arthropods, Annual Review of Physiology, 63 (2001) 327–357.
[14] Duman J.G., Olsen T.M., Thermal hysteresis protein activity in bacteria, fungi, and phylogenetically diverse plants, Cryobiology, 30 (1993) 322–328.
[15] Robles V., Valcarce D.G., Riesco M.F., The Use of Antifreeze Proteins in the Cryopreservation of Gametes and Embryos, Biomolecules, 9 (2019) 181.
[16] Ustun N.S., Turhan S., Antifreeze proteins: characteristics, function, mechanism of action, sources and application to foods, Journal of Food Processing and Preservation, 39 (2015) 3189–3197.
[17] Graham L.A., Liou Y.C., Davies P.L., Walker V.K., Hyperactive antifreeze protein from beetles, Nature, 388 (1997) 727-728.
[18] Patterson J.L., Duman J.G., The role of thermal hysteresis producing proteins in the low temperature tolerance and water balance of larvae of the mealworm, Tenebrio molitor, Journal of Experimental Biology, 74 (1978) 37–45.
[19] Dolev M.B., Braslavsky I., Davies P.L., Ice-Binding Proteins and Their Function, Annual Review of Biochemistry, 85 (2016) 515–542.
[20] National Center for Biotechnology Information, NCBI Database, (2025).
[21] Uniprot KB, Uniprot Database, (2025).
[22] Liou Y.C., Thibault P., Walker V.K., Davies P.L., Graham L.A., A Complex Family of Highly Heterogeneous and Internally Repetitive Hyperactive Antifreeze Proteins from the Beetle Tenebrio molitor, Biochemistry, 38 (1999) 11415–11424.
[23] Davies P.L., Sykes B.D., Antifreeze proteins, Current Opinion in Structural Biology, 7 (1997) 828–834.
[24] Graether S.P., Kuiper M.J., Gagne S.M., Walker V.K., Jia Z., Sykes B.D., Davies P.L., b-Helix structure and ice-binding properties of a hyperactive antifreeze protein from an insect, Nature, 406 (2000) 337-340.
[25] Graham L.A., Qin W., Lougheed S.C., Davies P.L., Walker V.K., Evolution of Hyperactive, Repetitive Antifreeze Proteins in Beetles, Journal of Molecular Evolution, 64 (2007) 1–13.
[26] Swanson W.J., Aquadro C.F., Positive Darwinian Selection Promotes Heterogeneity Among Members of the Antifreeze Protein Multigene Family, Journal of Molecular Evolution, 54 (2002) 403-410.
[27] Nabozhenko M.V., Personal communication, (2020).
[28] Keskin B., Ferrer J., First record of Xanthomus cf. ovulus Seidlitz, 1895 (Coleoptera: Tenebrionidae) from Turkey, Zoology in the Middle East, 39(1) (2006) 114-116.
[29] Nabozhenko M.V., Review of the Genus Cylindrinotus Faldermann, 1837 (Coleoptera: Tenebrionidae: Helopini), The Coleopterists Society Special Publication, 14 (2015) 101-114.
[30] Nabozhenko M.V., Keskin B., Revision of the genus Odocnemis Allard, 1876 (Coleoptera: Tenebrionidae: Helopini) from Turkey, the Caucasus and Iran with observations on feeding habits, Zootaxa, 4202(1) (2016) 1-97.
[31] Keskin B., Nabozhenko M.V., Keskin N.A., Taxonomic Review of The Genera Nalassus Mulsant, 1854 and Turkonalassus Gen. Nov. of Turkey (Coleoptera: Tenebrionidae), Annales Zoologici (Warszawa), 67(4) (2017) 725-747.
[32] Gough J., Karplus K., Hughey R., Chothia C., Assignment of Homology to Genome Sequences using a Library of Hidden Markov Models that Represent all Proteins of Known Structure, Journal of Molecular Biology, 313(4) (2001) 903-919.
[33] Motif Finder, Motif Finder Database, (2025).
[34] Waterhouse A., Bertoni M., Bienert S., Studer G., Tauriello G., Gumienny R., et al., SWISS-MODEL: homology modelling of protein structures and complexes, Nucleic Acids Research, 46 (2018) W296-W303.
[35] Nagano N., Ota M., Nishikawa K., Strong hydrophobic nature of cysteine residues in proteins, FEBS Letters, 458 (1999) 69-71.
[36] Hwang J., Kim B., Lee M.J., Kim E.J., Cho S.M., Lee S.G., et al., Importance of rigidity of ice-binding protein (FfIBP) for hyperthermal hysteresis activity and microbial survival, International Journal of Biological Macromolecules, 204 (2022) 485–499.
[37] Nam Y., Nguyen D.L., Hoang T., Kim B., Lee J.H., Do H., Engineered ice-binding protein (FfIBP) shows increased stability and resistance to thermal and chemical denaturation compared to the wildtype, Nature, 14 (2024) 3234.
[38] Liou Y.C., Daley M.E., Graham L.A., Kay C.M., Walker V.K., Sykes B.D., Davies P.L., Folding and Structural Characterization of Highly Disulfide-Bonded Beetle Antifreeze Protein Produced in Bacteria, Protein Expression and Purification, 19 (2000) 148–157.
Başka bir talebiniz var mı? Bu referansların genel bir bibliyografyasını oluşturmamı veya belirli bir bölüme göre (örneğin protein yapısı vs.) gruplandırmamı ister misiniz?

Details

Primary Language

English

Subjects

Structural Biology

Journal Section

Research Article

Authors

Didem Mimiroğlu
0000-0003-2838-9719
Türkiye

Sema Zabcı ^*
0000-0002-8886-0077
Türkiye

Publication Date

December 30, 2025

Submission Date

May 26, 2025

Acceptance Date

November 18, 2025

Published in Issue

Year 2025 Volume: 46 Number: 4

DOI

https://doi.org/10.17776/csj.1706951

IZ

https://izlik.org/JA48LB72XZ

Cite

RIS / Bibtex

APA

Mimiroğlu, D., & Zabcı, S. (2025). Understanding of Protein Adhesion to PLGA Through Molecular Docking Analysis. Cumhuriyet Science Journal, 46(4), 689-697. https://doi.org/10.17776/csj.1706951