Combinatorial Peptide Library Protocols

1. Front Matter

   Pages i-xiii

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2. Synthesis of a One-Bead One-Compound Combinatorial Peptide Library

   • Kit S. Lam, Michal Lebl

   Pages 1-6

3. Enzyme-Linked Calorimetric Screening of a One-Bead One-Compound Combinatorial Library

   • Kit S. Lam

   Pages 7-12

4. Synthesis and Screening of Positional Scanning Combinatorial Libraries

   • Colette T. Dooley, Richard A. Houghten

   Pages 13-24

5. Synthesis and Screening of Peptide Libraries on Continuous Cellulose Membrane Supports

   • Achim Kramer, Jens Schneider-Mergener

   Pages 25-39

6. Peralkylation

   • John M. Ostresh, Barbara Dörner, Richard A. Houghten

   Pages 41-49

7. Introduction to Combinatorial Solid-Phase Assays for Enzyme Activity and Inhibition

   • Morten Meldal

   Pages 51-57

8. Preparation of Biocompatible Resins for Library Syntheses

   • Morten Meldal

   Pages 59-63

9. Intramolecular Fluorescence-Quenched Substrate Libraries

   • Morten Meldal

   Pages 65-74

10. The Solid-Phase Enzyme Inhibitor Library Assay

    • Morten Meldal

    Pages 75-82

11. Determination of Peptide Substrate Motifs for Protein Kinases Using a “One-Bead One-Compound” Combinatorial Library Approach

    • Kit S. Lam

    Pages 83-86

12. The Use of Peptide Library for the Determination of Kinase Peptide Substrates

    • Zhou Songyang, Lewis C. Cantley

    Pages 87-98

13. Analysis of Protein Kinase Substrate Specificity by the Use of Peptide Libraries on Cellulose Paper (SPOT-Method)

    • Werner J. Tegge, Ronald Frank

    Pages 99-106

14. Generation of Multiuse Peptide Libraries for Functional Screenings

    • Channa K. Jayawickreme, Shiranthi P. Jayawickreme, Michael R. Lerner

    Pages 107-118

15. Functional Screening of Multiuse Peptide Libraries Using Melanophore Bioassay

    • Channa K. Jayawickreme, Shiranthi P. Jayawickreme, Michael R. Lerner

    Pages 119-128

16. The Basic Structure of Filamentous Phage and Its Use in the Display of Combinatorial Peptide Libraries

    • Shmuel Cabilly

    Pages 129-136

17. Construction and Use of a 20-mer Phage Display Epitope Library

    • Baruch Stern, Jonathan M. Gershoni

    Pages 137-154

18. Construction of Disulfide-Constrained Random Peptide Libraries Displayed on Phage Coat Protein VIII

    • Alessandra Luzzago, Franco Felici

    Pages 155-164

19. Conformational Mimicry Through Random Constraints Plus Affinity Selection

    • Guangming Zhong

    Pages 165-173

20. The Use of Combinatorial Libraries to Identify Ligands That Interact with Surface Receptors in Living Cells

    • Shmuel Cabilly, Judith Heldman, Eliahu Heldman, Ephraim Katchalski-Katzir

    Pages 175-183

During the course of evolution, an imbalance was created between the rate of vertebrate genetic adaptation and that of the lower forms of living organisms, such as bacteria and viruses. This imbalance has given the latter the advantage of generating, relatively quickly, molecules with unexpected structures and features that carry a threat to vertebrates. To compensate for their weakness, vertebrates have accelerated their own evolutionary processes, not at the level of whole organism, but in specialized cells containing the genes that code for antibody molecules or for T-cell receptors. That is, when an immediate requirement for molecules capable of specific interactions arose, nature has preferred to speed up the mode of Darwinian evolution in pref- ence to any other approach (such as the use of X-ray diffraction studies and computergraphic analysis). Recently, Darwinian rules have been adapted for test tube research, and the concept of selecting molecules having particular characteristics from r- dom pools has been realized in the form of various chemical and biological combinatorial libraries. While working with these libraries, we noticed the interesting fact that when combinatorial libraries of oligopeptides were allowed to interact with different selector proteins, only the actual binding sites of these proteins showed binding properties, whereas the rest of the p- tein surface seemed "inert. " This seemingly common feature of protein- having no extra potential binding sites--was probably selected during evolution in order to minimize nonspecific interactions with the surrounding milieu.

• Weizmann Institute of Science, Rehovot, Israel

  Shmuel Cabilly

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