During the last decade, there have been enormous advances in our knowledge of glycoproteins and the stage has been set for the biotechnological production of many of them for therapeutic use. These advances are reviewed, with special emphasis on the structure and function of the glycoproteins (excluding the proteoglycans). Current methods for structural analysis of glycoproteins are surveyed, as are novel carbohydrate-peptide linking groups, and mono- and oligo-saccharide constituents found in these macromolecules. The possible roles of the carbohydrate units in modulating the physicochemical and biological properties of the parent proteins are discussed, and evidence is presented on their roles as recognition determinants between molecules and cells, or cell and cells. Finally, examples are given of changes that occur in the carbohydrates of soluble and cell-surface glycoproteins during differentiation, growth and malignancy, which further highlight the important role of these substances in health and disease.

Protein glycosylation. Structural and functional aspects.

Despite the omnipresence of protein glycosylation in nature, little is known about how the attachment of carbohydrates affects peptide and protein activity. One reason is the lack of a straightforward method to access biologically relevant glycopeptides and glycoproteins. The isolation of homogeneous glycopeptides from natural sources is complicated by the heterogeneity of naturally occuring glycoproteins. It is chemical and chemoenzymatic synthesis that is meeting the challenge to solve this availability problem, thus playing a key role for the advancement of glycobiology. The current art of glycopeptide synthesis, albeit far from being routine, has reached a level of maturity that allows for the access to homogeneous and pure material for biological and medicinal research. Even the ambitious goal of the total synthesis of an entire glycoprotein is within reach. It is demonstrated that with the help of synthetic glycopeptides the effects of glycosylation on protein structure and function can be studied in molecular detail. For example, in immunology, synthetic (tumour-specific) glycopeptides can be used as immunogens to elicit a tumour-cell-specific immune response. Again, synthetic glycopeptides are an invaluable tool to determine the fine specificity of the immune response that can be mediated by both carbohydrate-specific B and T cells. Furthermore, selected examples for the use of synthetic glycopeptides as ligands of carbohydrate-binding proteins and as enzyme substrates or inhibitors are presented.

Glycopeptide synthesis and the effects of glycosylation on protein structure and activity.

Intramolecular O-Glycoside Bond Formation

The microbe-host interface is currently in focus because of attempts to develop infection therapy in humans based on either natural receptor saccharide (respiratory and gastrointestinal disease) or sophisticated sialic acid analogues designed from crystal structures (influenza). Most of the known host receptors for microbes are glycoconjugates, and the diversity and selectivity of host tissue glycosylation allow for the tropism of infections. However, among the many binding specificities detected so far, the biological role has been proven only in a few infectious model systems. The existence of multiple specificities of a single microbe is both a complicating factor and a challenge, requiring expanded research with a special demand on glycoscience.

Meaning and therapeutic potential of microbial recognition of host glycoconjugates

Use of lectins as diagnostic and therapeutic tools for cancer.

Glycobiology: a growing field for drug design

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Glycobiology: a growing field for drug design