Enzymatic mono-pegylation of glucagon-like peptide 1 towards long lasting treatment of type 2 diabetes

Results in Pharma Sciences

Volumn 2, Issue 1, 2012, Pages 58-65

  Selis, Fabio ^a   Schrepfer, Rodolfo ^b   Sanna, Riccardo ^b   Scaramuzza, Silvia ^a   Tonon, Giancarlo ^b   Dedoni, Simona ^c   Onali, Pierluigi ^c   Orsini, Gaetano ^b   Genovese, Stefano ^b  

^a INSTITUTE OF GENETICS AND BIOPHYSICS ADRIANO BUZZATI TRAVERSO   (Italy)

^b IRCCS MULTIMEDICA   (Italy)

^c UNIVERSITY OF CAGLIARI   (Italy)

Author keywords

Enzymatic pegylation; GLP 1; Pegylated GLP 1; Transglutaminase; Type 2 diabetes

Indexed keywords

GLUCAGON LIKE PEPTIDE 1 [7-36] AMIDE; GLUCAGON LIKE PEPTIDE 1 RECEPTOR; GLUTAMINE; MACROGOL; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; AREA UNDER THE CURVE; ARTICLE; BIOLOGICAL ACTIVITY; CONTROLLED STUDY; DRUG BLOOD LEVEL; DRUG DELIVERY SYSTEM; DRUG FORMULATION; DRUG HALF LIFE; DRUG MECHANISM; DRUG POTENCY; DRUG RELEASE; DRUG STABILITY; INSULIN LIKE ACTIVITY; KIDNEY CLEARANCE; MALE; MAXIMUM PLASMA CONCENTRATION; MOUSE; NON INSULIN DEPENDENT DIABETES MELLITUS; NONHUMAN; ORAL GLUCOSE TOLERANCE TEST; PANCREAS ISLET BETA CELL; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; RAT;

EID: 84867454064     PISSN: None     EISSN: 22112863     Source Type: Journal    
DOI: 10.1016/j.rinphs.2012.09.001     Document Type: Article

References (24)

1. Holst J.J., Deacon C.F., Vilsbøll T., Krarup T., Madsbad S. Glucagon-like peptide-1, glucose homeostasis and diabetes. Trends in Molecular Medicine 2008, 14:161-168.
2. Holst J.J. The physiology of glucagon-like peptide 1. Physiological Reviews 2007, 87:1409-1439.
3. Mayo K.E., Miller L.J., Bataille D., Dalle S., Goke B., Thorens B., Drucker D.J. Glucagon receptor family. Pharmacological Reviews 2003, 55:167-194.
4. Arhèn B. Islet G protein-coupled receptors as potential targets for treatment of type 2 diabetes. Nature Reviews Drug Discovery 2009, 8:369-385.
5. Ban K., Hossein Noyan-Ashraf M., Hoefer J., Bolz S., Drucker D.J., Husain M. Cardioprotective and vasodilatory actions of glucagon-like peptide 1 receptor are mediated through both glucagon-like peptide 1 receptor-dependent and -independent pathways. Circulation 2008, 117:2340-2350.
6. Davidson M.B., Bate G., Kirkpatrick P. Exenatide. Nature Reviews Drug Discovery 2005, 4:713-714.
7. Laemmli U.K. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
8. Folk J., Cole P.W. Transglutaminase: mechanicistic features of the active site as determined by kinetic and inhibitor studies. Biochimica et Biophysica Acta 1966, 122:244-264.
9. Gallwitz B., Witt M., Paetzold G., Morys-Wortmann C., Zimmermann B., Eckart K., Fölsch U.R., Schmidt W.E. Structure/activity characterization of glucagon-like peptide-1. European Journal of Biochemistry 1994, 225:1151-1156.
10. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding. Analytical Biochemistry 1976, 72:248-254.
11. Salomon Y., Londos C., Rodbell M A highly sensitive adenylyl cyclase assay. Analytical Biochemistry 1974, 58:541-548.
12. Green B.D., Gault V.A., Mooney M.H., Irwin N., Bailey C.J., Harriot P., Greer B., Flatt P.R., OHarte F.P.M. Novel dipeptidyl peptidase IV resistant analogues of glucagon-like peptide-(7-36)-amide have preserved biological activities in vitro conferring improved glucose-lowering action in vivo. Journal of Molecular Endocrinology 2003, 31:529-540.
13. Pan C.Q., Buxton J.M., Yung S.L., Tom I., Yang L., Chen H., MacDougall M., Bell A., Claus T.H., Clairmont K.B., Whelan J.P. Design of a long acting peptide functioning as both a glucagon-like peptide-1 receptor agonist and a glucagon receptor antagonist. Journal of Biological Chemistry 2006, 18:12506-12515.
14. Pasut G., Veronese F.M. PEGylation for improving the effectiveness of therapeutic biomolecules. Drugs Today (Barc) 2009, 45:687-695.
15. Parkes D., Joda C., Smith P., Nayak S., Rinehart L., Gingerich R., Chen K., Young A. Pharmacokinetic actions of exendin-4 in the rat: comparison with glucagon-like peptide-1. Drug Development Research 2001, 53:260-267.
16. Veronese F.M., Pasut G. PEGylation, successful approach to drug delivery. Drug Discovery Today 2005, 10:1451-1458.
17. Kinstler O.B., Gabriel N.E., Farrar C.E., DePrince R.B. N-terminally chemically modified protein composition and methods. US Pat. no. 5,985,265; 1999.
18. Hareter A., Hoffmann E., Bode H-P., Goke B., Goke R. The positive charge of the imidazole side chain of histidine7 is crucial for GLP-1 action. Endocrine Journal 1997, 44:701-705.
19. Youn Y.S., Chae S.Y., Lee S., Jeon J.E., Shin H.G. Evaluation of therapeutic potentials of site-specific PEGylated glucagon-like peptide-1 isomers as type 2 anti-diabetic treatment. Insulinotropic activity, glucose-stabilizing capability and proteolytic stability. Biochemical Pharmacology 2007, 73:84-93.
20. Drucker D.J., Nauk M.A. The incretin system: glucagon-like peptide-1 receptor agonist and dipeptidyl peptidase-4 inhibitors in type 2 diabetes. Lancet 2006, 368:1696-1705.
21. Sato H. Enzymatic procedure for site-specific pegylation of proteins. Advanced Drug Delivery Reviews 2002, 54:487-504.
22. Fontana A., Spolaore B., Mero A., Veronese F.M. Site-specific modification and PEGylation of pharmaceutical proteins mediated by transglutaminase. Advanced Drug Delivery Reviews 2008, 60:13-28.
23. Thornton K., Gorenstein D.G. Structure of glucagon-like peptide (7-36) amide in dodecylphosphocholine micelle as determined by 2D NMR. Biochemistry 1994, 33:3532-3539.
24. Adelhorst K., Hedegaard B.B., Knudsen L.B., Kirks O. Structure-activity studies of glucagon-like peptide-1. Journal of Biological Chemistry 1994, 269:6275-6278.