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1

Conformational stability of six truncated cHMG1a proteins studied in their mixture by H/D exchange and electrospray ionization mass spectrometry.

100%

Petry I., Wiśniewski J. R., Szewczuk Z.

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2001

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vol. 48

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issue 4

1131-1136

EN

The high mobility group (HMG) proteins are abundant non-histone components of eukaryotic chromatin. The presence of C-terminal acidic tails is a common feature of the majority of HMG proteins. Although the biological significance of the acidic domains is not clear, they are conferring conformational and metabolic stability to the proteins in vitro. Moreover, the length and net charge of the acidic tails affect the strength of HMG protein interaction with DNA. Synthesis of an insect HMG protein by standard recombinant technology in bacteria leads to a mixture of the intact protein (cHMG1a-(1-113) (I)) and a series of its degradation products truncated at the C tail: cHMG1a-(1-111) (II); cHMG1a-(1-110) (III); cHMG1a-(1-109) (IV); cHMG1a-(1-108) (V); cHMG1a-(1-107) (VI); cHMG1a-(1-106) (VII). The proteins differ from each other only by the number of amino-acid residues at the C-terminal tail. We used H/D exchange mass spectrometry to characterize the stability of the proteins directly in their mixture. The results show that the proteins I-V and VII have very similar conformations. The protein VI is less compact and exchanges its protons faster than the others. It may be concluded that the C-terminal tail influences the conformation of the cHMG1a protein and that individual residues in this part of the protein play a key role in its compactness.

2

Design, synthesis and biological evaluation of a new bridged immunosuppressor.

88%

Szewczuk Z., Wilczyński A., Petry I., Siemion I. Z., Wieczorek Z.

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2001

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vol. 48

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issue 4

1147-1150

EN

A bridged peptide with the sequence: H-Thr-Pro-Gln-Arg-Gly-Asp-Val-γ-Abu-Asn-Asp-Gln-Glu-Glu-Thr-Thr-Gly-Val-Val-Ser-Thr-Pro-Leu-Ile-Arg-Asn-Gly-OH was designed to mimic the discontinuous epitope of the HLA-DQ molecule that might interact with CD4. The bridged peptide revealed distinct suppressory effect in the humoral immune response. This result supports our suggestion that the 164-172 region of the HLA-DQ molecule may enhance its interactions with coreceptors, possibly with CD4.

3

Evaluation of high temperature glycation of proteins and peptides by electrospray ionization mass spectrometry.

88%

Stefanowicz P., Boratyński J., Kańska U., Petry I., Szewczuk Z.

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2001

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vol. 48

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issue 4

1137-1141

EN

Recently Boratyński & Roy (Glycoconjugate J., 1998, 15, 131) described a fast and convenient procedure for the synthesis of glycoconjugates. In the present study we used ESI-MS and circular dichroism as tools to analyze non-enzymatic glycation prod- ucts of proteins and peptides. We discuss influence of reaction conditions on the rate of glycation of lysozyme. We analyze for the first time collision induced dissociation spectra of the obtained peptide conjugates.

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3 Acta Biochimica Polonica

3 2001

3 Petry I.

3 Szewczuk Z.

1 Boratyński J.

1 Kańska U.

1 Siemion I. Z.

1 Stefanowicz P.

1 Wieczorek Z.

1 Wilczyński A.

1 Wiśniewski J. R.

Conformational stability of six truncated cHMG1a proteins studied in their mixture by H/D exchange and electrospray ionization mass spectrometry.

Design, synthesis and biological evaluation of a new bridged immunosuppressor.

Evaluation of high temperature glycation of proteins and peptides by electrospray ionization mass spectrometry.