Search results for “phage display

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Open Access Pub publishes peer-reviewed, free-to-read open-access articles. Showing articles matching phage display — open any to read the full text, or download the PDF or XML.

2 articles
Peptides Open Access

Cyclic Peptides: Prominent Next Generation Targeted Therapies

Aug 2026
Reddy Pallerla ManjulaCorresponding author

Cyclic peptides are expected to play a significant role in the future of drug discovery and development. Their unique properties, such as enhanced target affinity, metabolic stability, and favorable pharmokinetic profiles, make them promising candidates for addressing complex therapeutic targets. Innovations in design and synthetic techniques, including phage display and genetic code expansion with noncanonical amino acids, are enabling the development of diverse cyclic peptide libraries. These advancements are expected to bridge the gap between traditional small molecules and biologics, offering significant promise in the treatment of complex diseases. The therapeutic potential of cyclic peptides is broad, with applications in various pharmacological activities, including antibiotics, antifungals, anticancer, and immunosuppressants. The number of cyclic peptide drugs under research has reached hundreds, some have entered the late clinical stage. With ongoing research, more cyclic peptide drugs are expected to be approved and enter the market in the future. Cyclic peptides are also valuable research tools, suitable for probes that selectively modulate target proteins or high affinity ligands for biomolecular imaging. The development of selection strategies and various cyclization strategies, non-natural amino acids, and functional building blocks further enhance their functionality and utility in drug development. In summary, Cyclic peptides are poised to be a valuable class of molecules in the future, with ongoing research and development efforts aimed at optimizing their properties and expanding their therapeutic applications. .

Isolation of Human Monoclonal scfv Antibody Specifically Recognizing the D2-5-Ht1a Heteromer.

Apr 2019 DOI 10.14302/issn.2377-2549.jndc-19-2736
Łukasiewicz SylwiaCorresponding author

Antibody phage display has become a useful technique for discovering and optimizing target-specific monoclonal antibodies suitable for many applications, including therapeutic ligands, which may act as direct pharmacological compounds or may be used as targeting ligands for controlled drug delivery. Recently, the D2-5-HT1A heteromer, which is formed by the dopamine D2 and serotonin 5-HT1A receptors has attracted attention as a potential target of antipsychotic drugs. Therefore, the aim of the study was to identify scFv monoclonal antibodies that are able to specifically recognize epitopes formed within the heteromer structure. Because both receptors are membrane proteins, it is important to conduct bio-panning experiments in the most natural conditions, in which the presented antigens (D2-5-HT1A heteromers) are in their native form and possibly in their best-preserved spatial structure. It has been shown here that phage display methodology can be successfully used in the preparation of monoclonal antibodies against dimers of membrane proteins. To separate phages specifically binding the D2-5-HT1A heteromer, the selection process using CHO+ cells with overexpression of both receptors was conducted. Phages that were bound to receptor monomers or other CHO-K1 cell surface proteins were eliminated as a result of negative selection by using CHO- cells expressing separate receptor monomers.

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