In silico analysis and structural modeling of zebu cattle α-lactalbumin milk protein
Year: 2026
Type: article
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.
Source: BMC Genomics
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
SDG: Zero hunger
Open Access status: gold
Estimated APC paid: $3,090
OpenAlex ID: W7216345105