TY - JOUR
T1 - An in silico, structural, and biological analysis of lactoferrin of different mammals
AU - da S. Vieira, Dielson
AU - Polveiro, Richard C.
AU - Butler, Thomas J.
AU - Hackett, Timothy A.
AU - Braga, Camila P.
AU - Puniya, Bhanwar Lal
AU - Teixeira, Weslen F.P.
AU - de M. Padilha, Pedro
AU - Adamec, Jiri
AU - Feitosa, Francisco L.F.
N1 - Funding Information:
The student was financed in part by the Coordenação de Aperfeiçoamento de Pessoal de Nível Superior – Brasil (CAPES) with the doctoral scholarship (2016/2017). The student has the support of the scholarship grant number 2017/22041-1 and 2019/02781-6 , from the São Paulo Research Foundation (FAPESP). T.A.H. is funded through UNL's Molecular Mechanisms of Diseases T32 Graduate Fellowship NIGMS T32GM107001 . We want to thank you to Dr. Flavio T. Sassaki and Dr. Alison T. M. Lima from the Federal University of Uberlandia, MG, Brazil for helping with the understanding process of modeling using some of the programs; and Dr. Tomás Helikar from the Department of Biochemistry in the University of Nebraska–Lincoln, for allowing the student to learn about bioinformatics. The authors also wish to acknowledge the Irish Centre for High-End Computing (ICHEC) for the provision of computational facilities and support for use of Kay in the homology modeling of the protein structures.
Funding Information:
The student was financed in part by the Coordena??o de Aperfei?oamento de Pessoal de N?vel Superior ? Brasil (CAPES) with the doctoral scholarship (2016/2017). The student has the support of the scholarship grant number 2017/22041-1 and 2019/02781-6, from the S?o Paulo Research Foundation (FAPESP). T.A.H. is funded through UNL's Molecular Mechanisms of Diseases T32 Graduate Fellowship NIGMS T32GM107001. We want to thank you to Dr. Flavio T. Sassaki and Dr. Alison T. M. Lima from the Federal University of Uberlandia, MG, Brazil for helping with the understanding process of modeling using some of the programs; and Dr. Tom?s Helikar from the Department of Biochemistry in the University of Nebraska?Lincoln, for allowing the student to learn about bioinformatics. The authors also wish to acknowledge the Irish Centre for High-End Computing (ICHEC) for the provision of computational facilities and support for use of Kay in the homology modeling of the protein structures.
Publisher Copyright:
© 2021 Elsevier B.V.
PY - 2021/9/30
Y1 - 2021/9/30
N2 - Lactoferrin (LF) belongs to the family of transferrins having multifunctional roles associated with the immune system of animals. To follow the aims for this study was selected 20 sequences of LF from mammalian species to evaluate the chemical, biological, and structural properties. Bioinformatics approaches used programs such as MAFFT for sequence alignment; PartitionFinder and MrBayes for phylogenetic approaches; I-TASSER, PROCHECK, Molecular Operating Environment (MOE), SWISS Model server, Peptide DB and Expasy ProtParam to estimate the physicochemical properties, to model the protein and predicted secondary structures. A phylogenic analysis shows species with genetic similarities clustered by complexity and unique grouping between Capra hircus, Macaca mulatta, and Myotis lucifugus, since they presented more amino acids but not overall changes in the iron-binding sites or biological aspects. Structural deviations in these clusters obtained in LF from those species were found in residues 46 (position 406-450), that is part of alpha-helix, and 37 (position 295-331), that is part of the beta-sheets. Our predicted model can be used to investigate more about structural aspects of LF and be applied for medicinal research.
AB - Lactoferrin (LF) belongs to the family of transferrins having multifunctional roles associated with the immune system of animals. To follow the aims for this study was selected 20 sequences of LF from mammalian species to evaluate the chemical, biological, and structural properties. Bioinformatics approaches used programs such as MAFFT for sequence alignment; PartitionFinder and MrBayes for phylogenetic approaches; I-TASSER, PROCHECK, Molecular Operating Environment (MOE), SWISS Model server, Peptide DB and Expasy ProtParam to estimate the physicochemical properties, to model the protein and predicted secondary structures. A phylogenic analysis shows species with genetic similarities clustered by complexity and unique grouping between Capra hircus, Macaca mulatta, and Myotis lucifugus, since they presented more amino acids but not overall changes in the iron-binding sites or biological aspects. Structural deviations in these clusters obtained in LF from those species were found in residues 46 (position 406-450), that is part of alpha-helix, and 37 (position 295-331), that is part of the beta-sheets. Our predicted model can be used to investigate more about structural aspects of LF and be applied for medicinal research.
KW - Globular glycoprotein
KW - In silico
KW - Lactotransferrin
KW - Mammalians
KW - Milk proteins
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U2 - 10.1016/j.ijbiomac.2021.07.102
DO - 10.1016/j.ijbiomac.2021.07.102
M3 - Article
C2 - 34302867
AN - SCOPUS:85111890052
VL - 187
SP - 119
EP - 126
JO - International Journal of Biological Macromolecules
JF - International Journal of Biological Macromolecules
SN - 0141-8130
ER -