Multifunctional peptide biointerfaces

Lau, King Hang Aaron and Mukhtar, Asma; Elsawy, Mohamed A., ed. (2023) Multifunctional peptide biointerfaces. In: Peptide Bionanomaterials. Springer, Cham, pp. 515-537. ISBN 9783031293603 (https://doi.org/10.1007/978-3-031-29360-3_15)

[thumbnail of Lau-etal-PBDA-2022-Multifunctional-peptide-biointerfaces] Text. Filename: Lau_etal_PBDA_2022_Multifunctional_peptide_biointerfaces.pdf
Accepted Author Manuscript
Restricted to Repository staff only until 28 August 2024.
License: Strathprints license 1.0
Download (2MB) | Request a copy

Abstract

In creating useful devices for biomedical and other applications that come into contact with biological fluids, it is of great interest to mimic the multifaceted control of complex biomolecular and cell interactions observed in nature. On the molecular level, all such interactions involve surfaces and interfaces. In biology, this is often a cell membrane interface. In devices, this is the surface or interface of an artificial material, be it a nanoparticle or the surface of a biomaterial or biosensor. Multifunctional biointerfaces aim to provide simultaneous modulation of several biological signals. This chapter highlights the use of both linear and multi-armed peptide designs specifically conceived for such multifunctional surface applications. As shown by the studies reviewed, this dedicated strategy has met with considerable success, not least because even relatively short oligopeptide sequences, including cell-instructive and antimicrobial motifs, are being shown to be capable of diverse and robust bioactivities. Moreover, these sequences (and related peptidomimics) may be rationally combined and conveniently synthesized by standardized solid phase peptide synthesis. In addition, research into multifunctional peptide biointerfaces has been greatly aided by advances in simple and facile surface immobilization chemistries (e.g. SAMs and DOPA/polydopamine), as well as the realization that proteins possess native “antifouling” properties that can be mimicked by simple and mostly zwitterionic residue compositions to suppress non-specific interactions and enhance biorecognition binding. Overall, functionalization of biointerfaces with multifunctional peptides stands out as a powerful strategy to engineer protein-mimetic bioactivity on artificial materials and device surfaces, and great scope remains for the development of applications based on even more diverse peptide architectures as well as an expanded range of protein-mimetic biorecognition and multifunctionality.

  • Item type:Book Section
    ID code:82465
    Dates:
    Date
    Event
    30 August 2023
    Published
    29 August 2023
    Published Online
    27 September 2022
    Accepted
    Subjects:Science > Chemistry
    Department:Faculty of Science > Pure and Applied Chemistry
    Depositing user: Pure Administrator
    Date deposited:28 Sep 2022 09:30
    Last modified:08 Apr 2024 14:16
    URI:https://strathprints.strath.ac.uk/id/eprint/82465
CORE (COnnecting REpositories)