Analysis of mutations of defensin protein using accelerated molecular dynamics simulations
Plant defensins possess diverse biological functions that include antifungal and antibacterial activities and α-amylase and trypsin inhibitory properties. Two mutations, G9R and V39R, were confirmed to increase the antifungal activity of Raphanus sativus antifungal protein 2 (RsAFP2). Accelerated Mo...
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Published in | PloS one Vol. 15; no. 11; p. e0241679 |
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30.11.2020
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Abstract | Plant defensins possess diverse biological functions that include antifungal and antibacterial activities and α-amylase and trypsin inhibitory properties. Two mutations, G9R and V39R, were confirmed to increase the antifungal activity of Raphanus sativus antifungal protein 2 (RsAFP2). Accelerated Molecular Dynamics (aMD) were carried out to examine the conformational changes present in these RsAFP2 mutants, and its two closest homologs compared to the wild-type protein. Specifically, the root mean square fluctuation values for the eight cysteine amino acids involved in the four disulfide bonds were low in the V39R mutant compared to the wild-type. Additionally, analysis of the free energy change revealed that G9R and V39R mutations exert a neutral and stabilizing effect on RsAFP2 conformation, and this is supported by the observed lower total energy of mutants compared to the wild-type, suggesting that enhanced stability of the mutants. However, MD simulations to a longer time scale would aid in capturing more conformational state of the wild-type and mutants defensin protein. Furthermore, the aMD simulations on fungal mimic membranes with RsAFP2 and its mutants and homologs showed that the mutant proteins caused higher deformation and water diffusion than the native RsAFP2, especially the V39R mutant. The mutant variants seem to interact by specifically targeting the POPC and POPI lipids amongst others. This work highlights the stabilizing effect of mutations at the 9th and 39th positions of RsAFP2 and their increased membrane deformation activity. |
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AbstractList | Plant defensins possess diverse biological functions that include antifungal and antibacterial activities and α-amylase and trypsin inhibitory properties. Two mutations, G9R and V39R, were confirmed to increase the antifungal activity of Raphanus sativus antifungal protein 2 (RsAFP2). Accelerated Molecular Dynamics (aMD) were carried out to examine the conformational changes present in these RsAFP2 mutants, and its two closest homologs compared to the wild-type protein. Specifically, the root mean square fluctuation values for the eight cysteine amino acids involved in the four disulfide bonds were low in the V39R mutant compared to the wild-type. Additionally, analysis of the free energy change revealed that G9R and V39R mutations exert a neutral and stabilizing effect on RsAFP2 conformation, and this is supported by the observed lower total energy of mutants compared to the wild-type, suggesting that enhanced stability of the mutants. However, MD simulations to a longer time scale would aid in capturing more conformational state of the wild-type and mutants defensin protein. Furthermore, the aMD simulations on fungal mimic membranes with RsAFP2 and its mutants and homologs showed that the mutant proteins caused higher deformation and water diffusion than the native RsAFP2, especially the V39R mutant. The mutant variants seem to interact by specifically targeting the POPC and POPI lipids amongst others. This work highlights the stabilizing effect of mutations at the 9th and 39th positions of RsAFP2 and their increased membrane deformation activity. Plant defensins possess diverse biological functions that include antifungal and antibacterial activities and [alpha]-amylase and trypsin inhibitory properties. Two mutations, G9R and V39R, were confirmed to increase the antifungal activity of Raphanus sativus antifungal protein 2 (RsAFP2). Accelerated Molecular Dynamics (aMD) were carried out to examine the conformational changes present in these RsAFP2 mutants, and its two closest homologs compared to the wild-type protein. Specifically, the root mean square fluctuation values for the eight cysteine amino acids involved in the four disulfide bonds were low in the V39R mutant compared to the wild-type. Additionally, analysis of the free energy change revealed that G9R and V39R mutations exert a neutral and stabilizing effect on RsAFP2 conformation, and this is supported by the observed lower total energy of mutants compared to the wild-type, suggesting that enhanced stability of the mutants. However, MD simulations to a longer time scale would aid in capturing more conformational state of the wild-type and mutants defensin protein. Furthermore, the aMD simulations on fungal mimic membranes with RsAFP2 and its mutants and homologs showed that the mutant proteins caused higher deformation and water diffusion than the native RsAFP2, especially the V39R mutant. The mutant variants seem to interact by specifically targeting the POPC and POPI lipids amongst others. This work highlights the stabilizing effect of mutations at the 9.sup.th and 39.sup.th positions of RsAFP2 and their increased membrane deformation activity. Plant defensins possess diverse biological functions that include antifungal and antibacterial activities and α-amylase and trypsin inhibitory properties. Two mutations, G9R and V39R, were confirmed to increase the antifungal activity of Raphanus sativus antifungal protein 2 (RsAFP2). Accelerated Molecular Dynamics (aMD) were carried out to examine the conformational changes present in these RsAFP2 mutants, and its two closest homologs compared to the wild-type protein. Specifically, the root mean square fluctuation values for the eight cysteine amino acids involved in the four disulfide bonds were low in the V39R mutant compared to the wild-type. Additionally, analysis of the free energy change revealed that G9R and V39R mutations exert a neutral and stabilizing effect on RsAFP2 conformation, and this is supported by the observed lower total energy of mutants compared to the wild-type, suggesting that enhanced stability of the mutants. However, MD simulations to a longer time scale would aid in capturing more conformational state of the wild-type and mutants defensin protein. Furthermore, the aMD simulations on fungal mimic membranes with RsAFP2 and its mutants and homologs showed that the mutant proteins caused higher deformation and water diffusion than the native RsAFP2, especially the V39R mutant. The mutant variants seem to interact by specifically targeting the POPC and POPI lipids amongst others. This work highlights the stabilizing effect of mutations at the 9 th and 39 th positions of RsAFP2 and their increased membrane deformation activity. |
Audience | Academic |
Author | Mishra, Awdhesh Kumar Alqarawi, Abdulaziz A Pandey, Bharati Abd Allah, Elsayed Fathi Prajapati, Gopal Kumar Mohanta, Tapan Kumar Tyagi, Chetna Hashem, Abeer |
AuthorAffiliation | 4 Department of Biotechnology, Yeungnam University, Gyeongsan, Gyeongbuk, Republic of Korea 5 Botany and Microbiology Department, College of Science, King Saud University, Riyadh, Saudi Arabia 3 Department of Bio-Engineering, Birla Institute of Technology, Mesra, Ranchi, Jharkhand, India 2 Department of Microbiology, Faculty of Science and Informatics, University of Szeged, Szeged, Hungary University of Michigan, UNITED STATES 1 School of Biotechnology, Jawaharlal Nehru University, New Delhi, India 8 Natural and Medical Sciences Research Center, University of Nizwa, Nizwa, Oman 6 Mycology and Plant Disease Survey Department, Plant Pathology Research Institute, ARC, Giza, Egypt 7 Plant Production Department, College of Food and Agricultural Sciences, King Saud University, Riyadh, Saudi Arabia |
AuthorAffiliation_xml | – name: 5 Botany and Microbiology Department, College of Science, King Saud University, Riyadh, Saudi Arabia – name: 6 Mycology and Plant Disease Survey Department, Plant Pathology Research Institute, ARC, Giza, Egypt – name: 8 Natural and Medical Sciences Research Center, University of Nizwa, Nizwa, Oman – name: University of Michigan, UNITED STATES – name: 1 School of Biotechnology, Jawaharlal Nehru University, New Delhi, India – name: 2 Department of Microbiology, Faculty of Science and Informatics, University of Szeged, Szeged, Hungary – name: 4 Department of Biotechnology, Yeungnam University, Gyeongsan, Gyeongbuk, Republic of Korea – name: 3 Department of Bio-Engineering, Birla Institute of Technology, Mesra, Ranchi, Jharkhand, India – name: 7 Plant Production Department, College of Food and Agricultural Sciences, King Saud University, Riyadh, Saudi Arabia |
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CitedBy_id | crossref_primary_10_3390_ijms23169264 crossref_primary_10_3390_ijms24010483 crossref_primary_10_1016_j_copbio_2023_102926 |
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Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Current address: Promea Therapeutic Pvt. Limited, Patancheru, Hyderabad, India Competing Interests: The authors have declared that no competing interests exist. |
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SubjectTerms | Amino Acid Sequence Amino acids Antifungal activity Antifungal agents Biology and Life Sciences Chemical bonds Defensins Defensins - chemistry Defensins - genetics Deuterium - chemistry Disulfide bonds Free energy Fungicides Gene mutation Genetic research Homology Identification and classification Lipids Medicine and Health Sciences Membranes Molecular dynamics Molecular Dynamics Simulation Molecular Sequence Data Mutants Mutation Mutation - genetics Peptides Physical Sciences Plant proteins Properties Proteins Sequence Alignment Sequence Homology, Amino Acid Simulation Trypsin α-Amylase |
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Title | Analysis of mutations of defensin protein using accelerated molecular dynamics simulations |
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