Abstract
Proteins are vital for basically every known organism. Therefore
the investigation of their structure, the development of
a deeper understanding of protein–protein interactions and
the design of novel peptides, which selectively interact with
proteins are fields of active research. Small peptides consisting
of the 20 natural amino acids typically show high conformational
flexibility and a low ...
Abstract
Proteins are vital for basically every known organism. Therefore
the investigation of their structure, the development of
a deeper understanding of protein–protein interactions and
the design of novel peptides, which selectively interact with
proteins are fields of active research. Small peptides consisting
of the 20 natural amino acids typically show high conformational
flexibility and a low in-vivo stability which hampers
their application as tools in medicinal diagnostics or molecular
biology. One very versatile strategy to overcome such
drawbacks is the use of peptidomimetics. These are small molecules which mimic natural peptides or proteins and thus
produce the same biological effects as their natural role models.
As the field of peptidomimetics is developing fast this
review can only provide selected approaches together with
examples and is not intended to be comprehensive. We focus
on the discussion of amino acid modifications, backbone
modifications, global restrictions by cyclisation and on synthetic
backbone scaffolds.
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