In silico analysis and structural modeling of zebu cattle α-lactalbumin milk protein
Abstract
Background: Milk production in cattle is a trait of significant economic importance, especially in dairy farming. α-Lactalbumin (α-LA) plays a crucial role in lactose synthesis, a key determinant of milk volume. Zebu cattle ( Bos indicus ), predominantly in tropical and sub-tropical regions, exhibit differences in milk production compared to Bos taurus breeds, often attributed to genetic and environmental factors. Understanding the structural attributes of α-LA protein in Zebu cattle provides a clue in improving milk production through selective breeding or biotechnological application studies. This study aimed to retrieve the target protein sequence, perform computational analysis, and structurally model Zebu cattle α-LA to evaluate its unique characteristics and potential for milk production traits and protein function.
Methodology: α-LA of zebu cattle was retrieved from the UniProt protein database in FASTA format and imported to NCBI BLAST for a similarity search. Expasy-ProtParam was used to evaluate physicochemical properties. Secondary structure prediction, multiple sequence alignment, homology modeling, and model quality evaluations were performed. Structure visualization was performed PyMOL and Discovery Studio.
Result: The physicochemical characteristics results showed that the molecular weight (16201.75 Da), isoelectric point (4.79), extinction coefficient (27960), and instability index (27.44) indicate the stability of the target protein. The results for the secondary structure of α-LA varied among different prediction tools, with different values for α-helix, random coil, and β-sheet. Intrinsic disorder was predicted as four disordered segments, where amino acid residues (positions 1 to 3, 82 to 89, and 139 to 142) were disordered, and the other residue positions were ordered and able to contribute to the stability of the protein structure. The predicted model showed structural similarity, with sequence identity of 99.19% and a query coverage of 87%, respectively, compared to Bos taurus (PDB ID: 1f6s.6.A) α-LA. The model had valid metrics with structural similarity and qualified prediction characteristics. The predicted structure contained a Ca2+ with 5 residues within 4 Å (chain A: K.98, D.101, D.103, D.106, and D.107), with intra-protein interactions, and metal complexes were shown.
Conclusion and recommendation: Results showed that α-LA had stable structure, intrinsically ordered residues, conserved regions essential for lactose synthase binding, indicating functional similarity with Bos taurus. Further researches on molecular dynamics, functional pathways analysis, and protein network analysis swill be advisable to strengthen and further verify the findings.
Related
- JAK3-Mediated Structural Remodeling of β-Catenin Suppresses Epithelial-Mesenchymal Transition: Insights from In Silico Modeling.
- In Vitro Modeling of Sarcopenia-Related Pathology and Exercise-Associated Adaptations: Integration with In Silico Approaches
- Nomenclature, classification, and in-silico structural analysis of MSP1a variants of Anaplasma marginale
- Immunomodulatory Effects of Galleria mellonella and Alphitobius diaperinus Protein Digestates Generated Using a Modified INFOGEST Protocol - In Vitro and In Silico Evidence.
- In Silico Structural Dynamics and Downstream Bioprocess of Recombinant Human SUMO-IL-33
BibTeX
@article{gelayie2026silico,
title = {{In silico analysis and structural modeling of zebu cattle α-lactalbumin milk protein}},
author = {Desalegn Amsalu Gelayie and Bizuayehu Kerisew and Abebe Tesfaye Gessese and Yihune Bergushe},
journal = {BMC Genomics},
year = {2026},
month = oct,
doi = {10.1186/s12864-026-13388-1},
url = {https://link.springer.com/10.1186/s12864-026-13388-1},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - In silico analysis and structural modeling of zebu cattle α-lactalbumin milk protein
AU - Desalegn Amsalu Gelayie
AU - Bizuayehu Kerisew
AU - Abebe Tesfaye Gessese
AU - Yihune Bergushe
PY - 2026
DA - 2026/10/02
JO - BMC Genomics
DO - 10.1186/s12864-026-13388-1
UR - https://link.springer.com/10.1186/s12864-026-13388-1
AB - Background: Milk production in cattle is a trait of significant economic importance, especially in dairy farming. α-Lactalbumin (α-LA) plays a crucial role in lactose synthesis, a key determinant of milk volume. Zebu cattle ( Bos indicus ), predominantly in tropical and sub-tropical regions, exhibit differences in milk production compared to Bos taurus breeds, often attributed to genetic and environmental factors. Understanding the structural attributes of α-LA protein in Zebu cattle provides a clue in improving milk production through selective breeding or biotechnological application studies. This study aimed to retrieve the target protein sequence, perform computational analysis, and structurally model Zebu cattle α-LA to evaluate its unique characteristics and potential for milk production traits and protein function. Methodology: α-LA of zebu cattle was retrieved from the UniProt protein database in FASTA format and imported to NCBI BLAST for a similarity search. Expasy-ProtParam was used to evaluate physicochemical properties. Secondary structure prediction, multiple sequence alignment, homology modeling, and model quality evaluations were performed. Structure visualization was performed PyMOL and Discovery Studio. Result: The physicochemical characteristics results showed that the molecular weight (16201.75 Da), isoelectric point (4.79), extinction coefficient (27960), and instability index (27.44) indicate the stability of the target protein. The results for the secondary structure of α-LA varied among different prediction tools, with different values for α-helix, random coil, and β-sheet. Intrinsic disorder was predicted as four disordered segments, where amino acid residues (positions 1 to 3, 82 to 89, and 139 to 142) were disordered, and the other residue positions were ordered and able to contribute to the stability of the protein structure. The predicted model showed structural similarity, with sequence identity of 99.19% and a query coverage of 87%, respectively, compared to Bos taurus (PDB ID: 1f6s.6.A) α-LA. The model had valid metrics with structural similarity and qualified prediction characteristics. The predicted structure contained a Ca2+ with 5 residues within 4 Å (chain A: K.98, D.101, D.103, D.106, and D.107), with intra-protein interactions, and metal complexes were shown. Conclusion and recommendation: Results showed that α-LA had stable structure, intrinsically ordered residues, conserved regions essential for lactose synthase binding, indicating functional similarity with Bos taurus. Further researches on molecular dynamics, functional pathways analysis, and protein network analysis swill be advisable to strengthen and further verify the findings.
SN - 1471-2164
ER -