Chemoenzymatic synthesis of derivatives of a T-cell-stimulating peptide which carry tumor-associated carbohydrate antigens

2001 ◽  
pp. 880-885 ◽  
Author(s):  
Shaji K. George ◽  
Björn Holm ◽  
Celso A. Reis ◽  
Tilo Schwientek ◽  
Henrik Clausen ◽  
...  
Keyword(s):  
T Cell ◽  
Chemoenzymatic Synthesis ◽  
Carbohydrate Antigens ◽  
Derivatives Of ◽  
Tumor Associated Carbohydrate Antigens

scholarly journals Tumor-associated Carbohydrate Antigens: Sialyl Leaand T/Tn Antigens in Canine Mammary Tumors

2009 ◽  
Vol 46 (2) ◽  
pp. 222-226 ◽  
Author(s):  
M. Nowak ◽  
J. Madej ◽  
P. Dziégiel ◽  
W. Łopuszyński ◽  
A. Rodo ◽  
...  
Keyword(s):  
Mammary Tumors ◽  
Carbohydrate Antigens ◽  
Canine Mammary Tumors ◽  
Tumor Associated Carbohydrate Antigens

scholarly journals Major histocompatibility complex conformational epitopes are peptide specific.

1992 ◽  
Vol 176 (6) ◽  
pp. 1611-1618 ◽  
Author(s):  
B Catipović ◽  
J Dal Porto ◽  
M Mage ◽  
T E Johansen ◽  
J P Schneck
Keyword(s):  
Major Histocompatibility Complex ◽  
T Cell ◽  
Murine Cytomegalovirus ◽  
Major Histocompatibility ◽  
Cell Repertoire ◽  
Mhc Molecules ◽  
Histocompatibility Complex ◽  
Peptide Binding Groove ◽  
Binding Groove ◽  
Derivatives Of

Serologically distinct forms of H-2Kb are stabilized by loading cells expressing "empty" class I major histocompatibility complex (MHC) molecules with different H-2Kb binding peptides. The H-2Kb epitope recognized by monoclonal antibody (mAb) 28.8.6 was stabilized by ovalbumin (OVA) (257-264) and murine cytomegalovirus (MCMV) pp89 (168-176) peptides, but not by vesicular stomatic virus nucleoprotein (VSV NP) (52-59) and influenza NP (Y345-360) peptides. The H-2Kb epitope recognized by mAb 34.4.20 was stabilized by VSV NP (52-59) peptide but not by OVA (257-264), MCMV pp89 (168-176), or influenza NP (Y345-360) peptides. Immunoprecipitation of H-2Kb molecules from normal cells showed that 28.8.6 and 34.4.20 epitopes were only present on a subset of all conformationally reactive H-2Kb molecules. Using alanine-substituted derivatives of the VSV peptide, the 28.8.6 epitope was completely stabilized by substitution of the first residue and partially stabilized by substitution of the third or the fifth residues in the peptides. These results indicate that distinct conformational MHC epitopes are dependent on the specific peptide that occupies the antigenic peptide binding groove on individual MHC molecules. The changes in MHC epitopes observed may also be important in understanding the diversity of T cell receptors used in an immune response and the influence of peptides on development of the T cell repertoire.

scholarly journals Targeting tumor-associated carbohydrate antigens: a phase I study of a carbohydrate mimetic-peptide vaccine in stage IV breast cancer subjects

Oncotarget ◽  
2017 ◽  
Vol 8 (58) ◽  
pp. 99161-99178 ◽  
Author(s):  
Laura F. Hutchins ◽  
Issam Makhoul ◽  
Peter D. Emanuel ◽  
Angela Pennisi ◽  
Eric R. Siegel ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Phase I ◽  
Phase I Study ◽  
Peptide Vaccine ◽  
Stage Iv ◽  
Carbohydrate Antigens ◽  
Mimetic Peptide ◽  
Stage Iv Breast Cancer ◽  
Tumor Associated Carbohydrate Antigens

scholarly journals Chemoenzymatic Synthesis and Some Biological Properties of O-phosphoryl Derivatives of (E)-resveratrol

2008 ◽  
Vol 3 (10) ◽  
pp. 1934578X0800301 ◽  
Author(s):  
Danilo Aleo ◽  
Venera Cardile ◽  
Rosa Chillemi ◽  
Giuseppe Granata ◽  
Sebastiano Sciuto
Keyword(s):  
Prostate Cancer ◽  
Cancer Cells ◽  
Binding Affinity ◽  
Spectroscopic Investigation ◽  
Biological Properties ◽  
Chemoenzymatic Synthesis ◽  
Prostate Cancer Cells ◽  
Phosphoramidite Chemistry ◽  
Protective Groups ◽  
Derivatives Of

3- O-, 3,5-di- O- and 4′- O-phosphoryl derivatives of ( E)-resveratrol have been obtained following a chemoenzymatic strategy. Variedly acylated resveratrol derivatives have been obtained first by exploiting regioselective properties of Pseudomonas cepacea or Candida antarctica lipases in organic solvents. Each acyl-resveratrol was then phosphorylated by the phosphoramidite chemistry protocol and in sequence freed of protective groups, affording the desired O-phosphoryl derivative. Following UV-absorption spectroscopic investigation on the interaction of the newly synthesized compounds with DNA, 4′- O-phosphorylresveratrol exhibited the best binding affinity. As a result of cytotoxicity tests, 3- O-phosphorylresveratrol was more active than resveratrol against DU 145 prostate cancer cells.

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