Design of Tetra-Peptide Ligands of Antibody Fc Regions Using In Silico Combinatorial Library Screening

Marko Jukič (Avtor), Sebastjan Kralj (Avtor), Anja Kolarič (Avtor), Urban Bren (Avtor)

Povzetek

Abstract Peptides, or short chains of amino-acid residues, are becoming increasingly important as active ingredients of drugs and as crucial probes and/or tools in medical, biotechnological, and pharmaceutical research. Situated at the interface between small molecules and larger macromolecular systems, they pose a difficult challenge for computational methods. We report an in silico peptide library generation and prioritization workflow using CmDock for identifying tetrapeptide ligands that bind to Fc regions of antibodies that is analogous to known in vitro recombinant peptide libraries’ display and expression systems. The results of our in silico study are in accordance with existing scientific literature on in vitro peptides that bind to antibody Fc regions. In addition, we postulate an evolving in silico library design workflow that will help circumvent the combinatorial problem of in vitro comprehensive peptide libraries by focusing on peptide subunits that exhibit favorable interaction profiles in initial in silico peptide generation and testing.

Ključne besede

peptidi;amino kisline;peptide design;in silico combinatorial library;peptide combinatorial library;peptide library design;high-throughput virtual screening;peptide molecular docking;antibody purification;peptide drug design;recombinant peptide libraries;

Podatki

Jezik:	Angleški jezik
Leto izida:	2023
Tipologija:	1.01 - Izvirni znanstveni članek
Organizacija:	UM FKKT - Fakulteta za kemijo in kemijsko tehnologijo
Založnik:	MDPI
UDK:	577
COBISS:	161574147
ISSN:	1424-8247
Št. ogledov:	210
Št. prenosov:	11
Ocena:	0 (0 glasov)
Metapodatki:

Ostali podatki

Sekundarni jezik:	Slovenski jezik
Sekundarne ključne besede:	peptidi;amino kisline;
Vrsta dela (COBISS):	Članek v reviji
Strani:	22 str.
Letnik:	ǂVol. ǂ16
Zvezek:	ǂno. ǂ8, [Article no.] 1170
Čas izdaje:	2023
DOI:	10.3390/ph16081170
ID:	21371965