Evidence map›Paper›PMID 39428935›Full record

ArticleCurrent molecular medicine2025

Evolutionary Sequences and Structural Information-driven Reconstruction of New Insulin-like Growth Factor-I Peptide Variants.

Nazam Khan, Maryam Althobiti, Raj Kumar Chinnadurai, Samir Alharbi, Rajender Kumar

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Article in Current molecular medicine, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

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1citing papers in PubMed
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1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Review
4 · The record

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5 · Who and what money

Authors and funding

5 authors.

Nazam KhanDepartment of Clinical Laboratory Sciences, College of Applied Medical Sciences, Shaqra University, Shaqra, Kingdom of Saudi Arabia.
Maryam AlthobitiDepartment of Clinical Laboratory Sciences, College of Applied Medical Sciences, Shaqra University, Shaqra, Kingdom of Saudi Arabia.
Raj Kumar ChinnaduraiMahatma Gandhi Medical Advanced Research Institute, Sri Balaji Vidyapeeth (Deemed-to-be-University), Pondicherry 607402, India.
Samir AlharbiDepartment of Clinical Laboratory Sciences, College of Applied Medical Sciences, Shaqra University, Shaqra, Kingdom of Saudi Arabia.
Rajender KumarDepartment of Chemistry, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of Technology, AlbaNova University Centre, Stockholm 106 91, Sweden.ORCID 0000-0002-3322-8621

Funding

Deanship of Scientific Research at Shaqra University SU-ANN-2023062
6 · The paper itself

Abstract

backgroundInsulin-like growth factor-I (IGF-I) is crucial in controlling cell growth, proliferation, and apoptosis. Its strong link to the development of cancers such as breast, prostate, lung, thyroid, and colorectal has positioned the IGF-1 signalling pathway as a promising target for novel cancer therapies. When activated, the IGF-1 receptor (IGF-1R) binds to IGF-I, playing a central role in promoting tumour cell growth and survival.

methodsIn this study, we combined evolutionary sequences with structural and functional data of IGF-1 to reconstruct ancestral sequences and design novel IGF-1 peptide variants.

resultsThe insulin-like growth factor system exhibits a vast sequence diversity, yet it shares a similar structural topology with conserved three pairs of disulfide linkages. Our study reveals that IGF-1 is associated with the IGF system of cell surface receptors through protein-protein interactions. Reconstructed IGF-1 variants show similar structure fold to reported viral IGF-1 competitive antagonists.

conclusionThis new insight guides the design of novel natural IGF-1 mimic peptides. It enhances our understanding of IGF-1's functionality and opens new avenues for the development of therapeutic peptides and small molecules as anticancer agents.

Indexed as

Evolution, MolecularInsulin-Like Growth Factor IPeptidesAmino Acid SequenceHumansInsulin-Like PeptidesModels, MolecularProtein BindingReceptor, IGF Type 1Signal TransductionIGF1 protein, humanInsulin-Like Growth Factor IInsulin-Like PeptidesPeptidesReceptor, IGF Type 1ASRcancerHomo sapiens.IGF-IRinsulinInsulin-like growth factor-I

Identifiers

PMID39428935

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