Structure of IL-6 IL-6 is a 19–26 kDa pleiotropic cytokine composed of 212 amino acids. It has a four-helix bundle structure with two long and two short α-helices, stabilized by two disulfide bonds. IL-6
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Structure of EGFR EGFR (HER1/ErbB1) is a transmembrane glycoprotein receptor in the ErbB family of receptor tyrosine kinases (RTKs). Extracellular domain (ECD): Binds epidermal growth factor (EGF) and related ligands. Transmembrane domain
Read More... Structure of VEGFA Vascular Endothelial Growth Factor A (VEGFA) is a key member of the VEGF family and plays a crucial role in angiogenesis and vascular permeability. Dimeric glycoprotein: VEGFA forms a
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Structure of PD-1 Programmed Cell Death Protein 1 (PD-1) is a type I transmembrane protein belonging to the CD28 family of immune checkpoint receptors. It consists of: Extracellular domain: A single IgV-like
Read More... Screening technologies for cyclic peptide libraries based on gene encoding have significantly advanced, offering robust platforms for the discovery of bioactive peptides with potential therapeutic applications. Two prominent methodologies in this domain
Read More... The study “A minimalistic cyclic ice-binding peptide from phage display” presents a novel approach to identifying short peptides that mimic the function of naturally occurring ice-binding proteins (IBPs). IBPs, also known as
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The article “Advancement and applications of peptide phage display technology in biomedical science” provides a comprehensive overview of the evolution and diverse applications of phage display technology, particularly focusing on peptide libraries,
Read More... Phage display technology, introduced over 35 years ago, is a versatile in vitro method that allows the presentation of peptides and antibodies on the surface of bacteriophages. This technique has been instrumental
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