摘要:

AbstractThis review discusses various issues regarding vaccines; what are they and how they work, safety aspects, the role of adjuvants and carriers in vaccination, synthetic peptides as immunogens, and new technologies for vaccine development and delivery including the identification of novel adjuvants for mucosal vaccine delivery. There has been a recent increase of interest in the use of lipids and carbohydrates as adjuvants, and so a particular emphasis is placed on adjuvants derived from lipids or carbohydrates, or from both. Copyright © 2003 European Peptide Society and John Wiley&Sons, Ltd

ISSN:1075-2617    

DOI:10.1002/psc.467

出版商:John Wiley&Sons, Ltd.    

年代:2003

数据来源: WILEY

摘要:

AbstractFour trityl‐type (i.e. non‐substituted trityl‐, o‐Cl‐trityl‐, o‐F‐trityl‐ and p‐CN‐trityl‐) amidomethyl polystyrene resins were evaluated comparatively, in terms of the stability of the trityl‐ester bond in slightly acidic dichloromethane solutions, and the p‐CN‐trityl‐amidomethyl polystyrene resin was found to be the most stable of them. The above resins were applied, in parallel with Wang benzyl‐type resin, well known for its stability in mild acidic conditions, to the Fmoc solid phase synthesis of the 43‐amino acid residue long bioactive peptide thymosin beta‐4. Independent of their differences in acid sensitivity, the resins seemed to function equally well under the conditions used, since pure thymosin beta‐4 was obtained with a final yield of approximately 30% from each resin. The trityl‐type amidomethyl polystyrene resins were also applied, in parallel with the Wang resin, to the Fmoc solid phase synthesis of a bioactive peptide containing proline at itsC‐terminus, i.e. theN‐terminal tetrapeptide of thymosin beta‐4, AcSDKP. In this case, the best yield (87%) was obtained with the o‐Cl‐trityl‐amidomethyl polystyrene resin, which may be the resin of choice, of those studied, for the Fmoc solid phase peptide synthesis. Copyright ©

ISSN:1075-2617    

DOI:10.1002/psc.454

出版商:John Wiley&Sons, Ltd.    

年代:2003

数据来源: WILEY

摘要:

AbstractAccording to recent investigations, theC‐terminal domain of the tissue inhibitor of matrix metalloproteinases‐1 (TIMP‐1) is responsible for some biological effects that are independent of the enzyme‐inhibiting effect of theN‐terminal domain of the molecule. TheC‐terminal domain has been prepared for structure–biological activity investigations. After the chemical synthesis and the folding of the linear peptide, LC‐MS and MALDI‐MS analysis revealed that two isomers with different disulphide bond arrangements were formed. Since more than 30 folding experiments resulted in products with a very similar HPLC‐profile, it was concluded that in the absence of the TIMP‐1N‐terminal domain no entirely correct folding of theC‐terminal domain occurred. Furthermore, it was observed that, in spite of several purification steps, mercury(II) ions were bound to the 6SH‐linear peptide; it was demonstrated—using disulphide bonded TIMP‐1(Cys145‐Cys166) as a model—that mercury(II) ions can cause peptide degradation at pH 7.8 as well as in 0.1% trifluoroacetic acid. Copyright © 2003 European Pept

ISSN:1075-2617    

DOI:10.1002/psc.455

出版商:John Wiley&Sons, Ltd.    

年代:2003

数据来源: WILEY

摘要:

AbstractA heterodimeric napin‐like polypeptide was isolated fromBrassica parachinensisseeds with a procedure involving ion exchange chromatography on DEAE‐cellulose, affinity chromatography on Affi‐gel blue gel, FPLC‐ion exchange chromatography on Mono S and FPLC‐gel filtration on Superdex 75. TheN‐terminal sequence of the 5 kDa subunit of the polypeptide (PAGPFRIPKKRKKEE) showed high homology with other 2S storage proteins like napins and albumins. The polypeptide potently inhibited translation in a cell free system with an IC50of 6.2 nM. The translation‐inhibiting activity of the polypeptide was relatively stable in the pH range 6–11 and in the temperature range 10–50°C. Copyright © 2003 European Peptide Society and J

ISSN:1075-2617    

DOI:10.1002/psc.460

出版商:John Wiley&Sons, Ltd.    

年代:2003

数据来源: WILEY

摘要:

AbstractIn this paper the NMR secondary chemical shifts, that are estimated from a set of 3D‐structures, are compared with the observed ones to appraise the behaviour of a known x‐ray diffraction structure (of the bovine pancreatic trypsin inhibitor protein) when various molecular dynamics are applied. The results of a 200 ps molecular dynamics under various conditions are analysed and different ways to modify the molecular dynamics are considered. With the purpose of avoiding the time‐consuming explicit representation of the solvent (water) molecules, an attempt was made to understand the role of the solvent and to develop an implicit representation, which may be refined. A simulation of hydrophobic effects in an aqueous environment is also proposed which seems to provide a better approximation of the observed solution structure of the protein. Copyright © 2003 European Peptide Society and John Wiley&Son

ISSN:1075-2617    

DOI:10.1002/psc.466

出版商:John Wiley&Sons, Ltd.    

年代:2003

数据来源: WILEY

摘要:

AbstractFifteen years ago it was shown that an α‐aminoisobutyric acid (Aib) residue is significantly more effective than anL‐Pro or aD‐amino acid residue in inducing β‐sheet disruption in short model peptides. As this secondary structure element is known to play a crucial role in the neuropathology of Alzheimer's disease, it was decided to check the effect of Aib (and other selected, helix inducer, Cα‐tetrasubstituted α‐amino acids) on the β‐sheet conformation adopted by a protected pentapeptide related to the sequence 17–21 of the β‐amyloid peptide. By use of FT‐IR absorption and1H NMR techniques it was found that the strong self‐association characterizing the pentapeptide molecules in weakly polar organic solvents is completely abolished by replacing a single residue with Aib or one of its congeners. Copyright © 2003 European Peptide Soci

ISSN:1075-2617    

DOI:10.1002/psc.503

出版商:John Wiley&Sons, Ltd.    

年代:2003

数据来源: WILEY