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Instruments / Technical Area	Publication Details	Published	Actions
	DypB peroxidase for aflatoxin removal: New insights into the toxin degradation process V. Mangini , E. Rosini , R. Caliandro , G. F. Mangiatordi , P. Delre , A. G. Sciancalepore , L. Pollegioni , M. Haidukowski , M. Mazzorana , M.w. Sumarah , J. B, Renaud , R. Flaig , G. Mulè , Benny D. Belviso , M. Loi Chemosphere 51 DOI: 10.1016/j.chemosphere.2023.140826 Show Abstract ▼ Abstract: Aflatoxin B1 (AFB1) is one of the most potent carcinogens and a widespread food and feed contaminant. As for other toxins, many efforts are devoted to find efficient and environmentally-friendly methods to degrade AFB1, such as enzymatic treatments, thus improving the safety of food and feed products. In this regard, the dye decolorizing peroxidase of type B (DypB) can efficiently degrade AFB1. The molecular mechanism, which is required to drive protein optimization in view of the usage of DypB as a mycotoxin reduction agent in large scale application, is unknown. Here, we focused on the role of four DypB residues in the degradation of AFB1 by alanine-scanning (residues 156, 215, 239 and 246), which were identified from biochemical assays to be kinetically relevant for the degradation. As a result of DypB degradation, AFB1 converts into four products. Interestingly, the relative abundancy of these products depends on the replaced residues. Molecular dynamics simulations were used to investigate the role of these residues in the binding step between protein and manganese, a metal ion which is expected to be involved in the degradation process. We found that the size of the haem pocket as well as conformational changes in the protein structure could play a role in determining the kinetics of AFB1 removal and, consequently, guide the process towards specific degradation products.	Nov 2023
B21-High Throughput SAXS	Exploring the role of elongation Factor-Like 1 (EFL1) in Shwachman-Diamond syndrome through molecular dynamics Pietro Delre , Domenico Alberga , Abril Gijsbers , Nuria Sánchez-Puig , Orazio Nicolotti , Michele Saviano , Dritan Siliqi , Giuseppe Felice Mangiatordi Journal Of Biomolecular Structure And Dynamics DOI: 10.1080/07391102.2019.1704883 Diamond Proposal Number(s): [21741] Show Abstract ▼ Abstract: Shwachman-Diamond Syndrome (SDS) is an autosomal recessive disorder whose patients present mutations in two ribosome assembly proteins, the Shwachman-Bodian-Diamond Syndrome protein (SBDS) and the Elongation Factor-Like 1 (EFL1). Due to the lack of knowledge of the molecular mechanisms responsible for SDS pathogenesis, current therapy is nonspecific and focuses only at alleviating the symptoms. Building on the recent observation that EFL1 single-point mutations clinically manifest as SDS-like phenotype, we carried out comparative Molecular Dynamics (MD) simulations on three mutants, T127A, M882K and R1095Q and wild type EFL1. As supported by small angle X-ray scattering experiments, the obtained data improve the static EFL1 model resulting from the Cryo-electron microscopy and clearly show that all the mutants experience a peculiar rotation, around the hinge region, of domain IV with respect to domains I and II leading to a different conformation respect to that of wild type protein. This study supports the notion that EFL1 function is governed by an allosteric mechanism involving the concerted action of GTPase domain (domain I) and the domain IV and can help point towards new approaches to SDS treatment.	Dec 2019

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