Molecular interaction between small nuclear ribonucleoprotein polypeptide G and heat shock protein 70.14: a microscale thermophoresis exposition towards developing anti-cancer drugs.

Anti-cancer drug discovery Hsp70.14 SNRPG dissociation constant microscale thermophoresis protein-protein interactions proteostasis

Journal

American journal of translational research
ISSN: 1943-8141
Titre abrégé: Am J Transl Res
Pays: United States
ID NLM: 101493030

Informations de publication

Date de publication:
2022
Historique:
received: 23 02 2022
accepted: 25 07 2022
entrez: 17 10 2022
pubmed: 18 10 2022
medline: 18 10 2022
Statut: epublish

Résumé

Targeting protein-protein interactions (PPIs) linked to protein quality control (PQC) pathways as potential anti-cancer drug targets have unanimously widened biological insights and the therapeutic potential of PPIs as smart-drug discovery tools in cancer. PPIs between disease-relevant proteins associated with protein homeostasis in PQC pathways have been linked to improved mechanistic understanding associated with conformational abnormalities and impairment, cellular proteotoxicity, induced apoptosis, and pathogenesis in different types of cancers. In this context, PPIs between small nuclear ribonucleoprotein polypeptide G (SNRPG) and heat shock protein 70.14 (Hsp70.14) have attracted attention as potential smart drug discovery tools in cancer diagnostics and therapeutics. Validated evidence of high-quality biological data has shown the presence of the two proteins in different types of cancers including breast cancer. The links between SNRPG and Hsp70.14 in cancer-cell networks remain elusive, overlooked, and uncharacterized. In this study, we explored the interaction between the two oncogenic proteins using the MST-based assays. The results revealed a low K The results suggest a possible involvement between the two proteins in hostile tumour microenvironments. Furthermore, these findings offer a different therapeutic perspective that could pave the way for the creation of novel small molecule inhibitors as drugs for the treatment of cancer.

Sections du résumé

BACKGROUND BACKGROUND
Targeting protein-protein interactions (PPIs) linked to protein quality control (PQC) pathways as potential anti-cancer drug targets have unanimously widened biological insights and the therapeutic potential of PPIs as smart-drug discovery tools in cancer. PPIs between disease-relevant proteins associated with protein homeostasis in PQC pathways have been linked to improved mechanistic understanding associated with conformational abnormalities and impairment, cellular proteotoxicity, induced apoptosis, and pathogenesis in different types of cancers. In this context, PPIs between small nuclear ribonucleoprotein polypeptide G (SNRPG) and heat shock protein 70.14 (Hsp70.14) have attracted attention as potential smart drug discovery tools in cancer diagnostics and therapeutics. Validated evidence of high-quality biological data has shown the presence of the two proteins in different types of cancers including breast cancer. The links between SNRPG and Hsp70.14 in cancer-cell networks remain elusive, overlooked, and uncharacterized.
METHODOLOGY METHODS
In this study, we explored the interaction between the two oncogenic proteins using the MST-based assays.
RESULTS RESULTS
The results revealed a low K
CONCLUSIONS CONCLUSIONS
The results suggest a possible involvement between the two proteins in hostile tumour microenvironments. Furthermore, these findings offer a different therapeutic perspective that could pave the way for the creation of novel small molecule inhibitors as drugs for the treatment of cancer.

Identifiants

PMID: 36247303 PMC: PMC9556510
pubmed: 36247303
pmc: PMC9556510

Types de publication

Journal Article

Langues

eng

Pagination

6150-6162

Informations de copyright

AJTR Copyright © 2022.

Déclaration de conflit d'intérêts

None.

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Auteurs

Lloyd Mabonga (L)

Department of Biochemistry and Microbiology, University of Zululand KwaDlangezwa 3886, South Africa.

Paul Chukwudi Ikwegbue (PC)

Division of Immunology, Department of Pathology, Faculty of Health Sciences, University of Cape Town Cape Town, South Africa.

Priscilla Masamba (P)

Molecular Biophysics and Structural Biology (MBSB) Group, Department of Biochemistry, Faculty of Science, University of Johannesburg, Auckland Park Kingsway Campus South Africa.

Abidemi Paul Kappo (AP)

Molecular Biophysics and Structural Biology (MBSB) Group, Department of Biochemistry, Faculty of Science, University of Johannesburg, Auckland Park Kingsway Campus South Africa.

Classifications MeSH