Dataset Information

Efficient Cleavage of Permethylated Cyclodextrins.

ABSTRACT: The cleavage of a permethylated ?-cyclodextrin, that is, purity and chemical yield of a maltohexaose derivative thus obtained, was decisively affected by the reaction time. The matrix-assisted laser desorption ionization time-of-flight mass spectrometry spectra with synthetic data enable us to improve the cleavage reaction more efficiently. The optimized conditions developed in the present study allow us to cleave the permethylated ?-cyclodextrin to afford a maltooctaose derivative as a new synthetic building block in a high chemical yield.

SUBMITTER: Ishida Y

PROVIDER: S-EPMC6644737 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature

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Efficient Cleavage of Permethylated Cyclodextrins.

Ishida Yuki Y Fukuhara Gaku G

ACS omega 20180611 6

The cleavage of a permethylated α-cyclodextrin, that is, purity and chemical yield of a maltohexaose derivative thus obtained, was decisively affected by the reaction time. The matrix-assisted laser desorption ionization time-of-flight mass spectrometry spectra with synthetic data enable us to improve the cleavage reaction more efficiently. The optimized conditions developed in the present study allow us to cleave the permethylated γ-cyclodextrin to afford a maltooctaose derivative as a new synt ...[more]

PMID: 31458809

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Project description:BackgroundThe proteolytic maturation of the nuclear protein lamin A by the zinc metalloprotease ZMPSTE24 is critical for human health. The lamin A precursor, prelamin A, undergoes a multi-step maturation process that includes CAAX processing (farnesylation, proteolysis and carboxylmethylation of the C-terminal CAAX motif), followed by ZMPSTE24-mediated cleavage of the last 15 amino acids, including the modified C-terminus. Failure to cleave the prelamin A "tail", due to mutations in either prelamin A or ZMPSTE24, results in a permanently prenylated form of prelamin A that underlies the premature aging disease Hutchinson-Gilford Progeria Syndrome (HGPS) and related progeroid disorders.Methodology/principal findingsHere we have investigated the features of the prelamin A substrate that are required for efficient cleavage by ZMPSTE24. We find that the C-terminal 41 amino acids of prelamin A contain sufficient context to allow cleavage of the tail by ZMPSTE24. We have identified several mutations in amino acids immediately surrounding the cleavage site (between Y646 and L647) that interfere with efficient cleavage of the prelamin A tail; these mutations include R644C, L648A and N650A, in addition to the previously reported L647R. Our data suggests that 9 of the 15 residues within the cleaved tail that lie immediately upstream of the CAAX motif are not critical for ZMPSTE24-mediated cleavage, as they can be replaced by the 9 amino acid HA epitope. However, duplication of the same 9 amino acids (to increase the distance between the prenyl group and the cleavage site) impairs the ability of ZMPSTE24 to cleave prelamin A.Conclusions/significanceOur data reveals amino acid preferences flanking the ZMPSTE24 cleavage site of prelamin A and suggests that spacing from the farnesyl-cysteine to the cleavage site is important for optimal ZMPSTE24 cleavage. These studies begin to elucidate the substrate requirements of an enzyme activity critical to human health and longevity.

Dataset Information

Efficient Cleavage of Permethylated Cyclodextrins.

Publications

Efficient Cleavage of Permethylated Cyclodextrins.

Similar Datasets

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