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Streptomyces sp. CBMAI 2042 Extracts

ABSTRACT: Ethyl Acetate fraction of Streptomyces sp. CBMAI 2042 was investigated for identifying cyclodepsipeptides using electrospray ionisation tandem mass spectrometry (ESI-MS/MS). Without prior isolation, the structural determination was achieved on the basis of mass fragmentation pattern and comparison with the previously established data. The ESI-MS of the fraction in the positive ion mode gave clusters of singly and doubly charged molecular ion peaks. The ESI-MS spectrum showed peaks for the presence of the cyclodepsipeptides Valinomycin, Montanastatin and at least 5 structural analogues never reported before.

INSTRUMENT(S): 6550 Quadrupole Time-of-flight LC/MS (Agilent technologies)

ORGANISM(S): Streptomyces Sp. Cbmai 2042

SUBMITTER: Bruno Sacchetto Paulo

PROVIDER: MSV000083709 | MassIVE | Mon Apr 22 06:23:00 BST 2019

REPOSITORIES: MassIVE

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Project description:Fast photochemical oxidation of proteins (FPOP) footprinting is a structural mass spectrometry method that maps proteins by fast and irreversible chemical reactions. The position of oxidative modification reflects solvent accessibility and site reactivity and thus provides information about protein conformation, structural dynamics, and interactions. Bottom-up mass spectrometry is an established standard method to analyze FPOP samples. In the bottom-up approach, all forms of the protein are digested together by a protease of choice, which results in mixture of peptides from various subpopulations of proteins with varying degrees of photochemical oxidation. But, once the protein is already oxidized at least once, the spatial distribution of any consecutive oxidation no longer truly reflects initial protein solvent accessibility and residue reactivity, because the site preference of further oxidation may also be influenced by the changes caused by the prior oxidation. Thus, it would be interesting to obtain an assessment of the protein structure based on the FPOP data, by analyzing only singly oxidized protein populations. This requires utilization of more specific top-down mass spectrometry approaches. The key element of any top-down experiment is selection of a suitable method of ion isolation, excitation and fragmentation. Here we employ and compare collision-induced dissociation (CID), electron-transfer dissociation (ETD), and electron-capture dissociation (ECD) combined with multi continuous accumulation of selected ions (CASI). Singly oxidized subpopulation of FPOP labeled ubiquitin was used to optimize the method. The usefulness was then demonstrated further by using it to visualize structural changes induced by cofactor removal from holo/apo myoglobin system. The top-down data were compared with the literature and with the bottom-up data set obtained on the same samples. The top-down results were found to be in a good agreement, which indicates that monitoring singly FPOP oxidized ion population by top-down is a functional workflow for oxidative protein footprinting.

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Streptomyces sp. CBMAI 2042 Extracts

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