Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural and biochemical investigation into stable FGF2 mutants with novel mutation sites and hydrophobic replacements for surface-exposed cysteines.

PloS one - 1 Jan 2024

An Young Jun, Jung Ye-Eun, Lee Kyeong Won, Kaushal Prashant, Ko In Young, Shin Seung Min, Ji Sangho, Yu Wookyung, Lee Cheolju, Lee Won-Kyu, Cha Kiweon, Lee Jung-Hyun, Cha Sun-Shin, Yim Hyung-Soon

Abstract excerpt

Fibroblast growth factor 2 (FGF2) is an attractive biomaterial for pharmaceuticals and functional cosmetics. To improve the thermo-stability of FGF2, we designed two mutants harboring four-point mutations: FGF2-M1 (D28E/C78L/C96I/S137P) and FGF2-M2 (D28E/C78I/C96I/S137P) through bioinformatics, molecular thermodynamics, and molecular modeling. The D28E mutation reduced fragmentation of the FGF2 wild type during...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Substitution
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cysteine

Share to Fibroblast Growth Factor 2

Share to Hydrophobic and Hydrophilic Interactions

Share to Models, Molecular

Share to Protein Stability

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 39236042
DOI: 10.1371/journal.pone.0307499
PMCID: PMC11376533

Genes

FGF2

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural and biochemical investigation into stable FGF2 mutants with novel mutation sites and hydrophobic replacements for surface-exposed cysteines.PMID 39236042Read ↗

Application of bioinformatics and molecular dynamics simulation approaches for identification of fibroblast growth factor 10 analogues with potentially improved thermostability.Semantic proximity Read ↗

Highly stable mutants of human fibroblast growth factor-1 exhibit prolonged biological action.Semantic proximity Read ↗

Structure of a highly stable mutant of human fibroblast growth factor 1.Semantic proximity Read ↗

An empirical phase diagram approach to investigate conformational stability of "second-generation" functional mutants of acidic fibroblast growth factor-1.Semantic proximity Read ↗

Temperature-responsive structural reversibility of FGF21 and structure-based design of its variant with enhanced potencySemantic proximity Read ↗

Thermodynamic characterization of mutants of human fibroblast growth factor 1 with an increased physiological half-life.Semantic proximity Read ↗

Bioengineering an Ultra-Stable and Cost-Effective FGF2 (NGF2) with Extended Circulatory Half-Life for Next-Generation TherapeuticsSemantic proximity Read ↗

Characterization of the structural forces governing the reversibility of the thermal unfolding of the human acidic fibroblast growth factor.Semantic proximity Read ↗

Binding of human recombinant mutant soluble ectodomain of FGFR2IIIc to c subtype of FGFRs: implications for anticancer activity.Semantic proximity Read ↗

Increased thermal stability of FGF10 leads to ectopic signaling during developmentSemantic proximity Read ↗

Combination of engineering the substrate and Ca2+ binding domains of heparinase I to improve the catalytic activity.Semantic proximity Read ↗

Further characterization and engineering of a 11-amino acid motif for enhancing recombinant protein expressionSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.