How do peptides fold?

LifeTein Peptide — Fri, 15 Sep 2017 16:07:33 +0000

Short Peptide Folding

How does the amino acid sequence of a protein chain determine and maintain its 3D folded state? How do small proteins fold?

Short Peptide Folding

Many small proteins or miniproteins are peptides shorter than 40-50 residues with stable folding that contain secondary structure elements such as alpha helices and beta strands.

An autonomously folding, 35-residue, thermostable subdomain (HP36) of the villain headpiece is the smallest folded domain of a naturally occurring protein. Polypeptides simplify the protein-folding problem. They allow in-depth examinations of sequence-structure-stability relationships without using the complex larger proteins.

In this recent study, Rocklin et al. designed sequences intended to fold into desired structures. The novel proteins may be helpful in bioengineering or pharmacological applications.

Check the paper from here: https://goo.gl/Tregb7

http://science.sciencemag.org/content/357/6347/168

The post How do peptides fold? first appeared on LifeTein Peptide Blog.

LifeTein Peptide Cited in Cell

LifeTein Peptide — Tue, 18 Nov 2014 18:17:42 +0000

Peptide library is increasingly used to define antibody epitopes and substrate specificities of protein kinases. For epitope mapping, overlapping peptides are made to span the antigenic protein sequence. The antigenic determinant recognized by a monoclonal antibody can then be screened and defined. The alanine scanning method can also be used to assess that residue’s contribution to antibody binding and to determine which substitutions affect antibody recognition (mutational analysis). Unrelated synthetic peptides can be used to evaluate the antibody cross-reactivity.

Peptide by LifeTein Cited in Cell

Overlapping peptides from LifeTein were used to map the region of Fragment 3 by epitope mapping of anti-Fzd2 antibody. This anti-Fzd2 antibody was found to reduce tumor growth. Wnt signaling plays a critical role in colorectal cancer. Researchers found that Wnt receptor Frizzled2 (Fzd2) and its ligands Wnt5a/b are elevated in metastatic liver, lung, colon, and breast cancer cell lines. Their high level expression correlates with markers of epithelial-mesenchymal transition (EMT). By epitope mapping using synthetic peptides from LifeTein, the researchers mapped the epitope to a specific region. The antibody to Fzd2 was found to reduce cell migration and invasion. Targeting this pathway may provide a cure for patients with tumors expressing high amount of Fzd2 and Wnt5a/b. We have developed an antibody to Fzd2 that reduces cell migration and invasion and inhibits tumor growth and metastasis in xenografts. We propose that targeting this pathway could provide benefit for patients with tumors expressing high levels of Fzd2 and Wnt5a/b.

Cell, Volume 159, Issue 4, 6 November 2014, Pages 844–856, DOI: 10.1016/j.cell.2014.10.032 A Noncanonical Frizzled2 Pathway Regulates Epithelial-Mesenchymal Transition and Metastasis

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Our Services: COVID-19 Services & Products Custom Antibody Services Rush Peptide Synthesis Peptide Nucleic Acids (PNAs) Custom Peptide Synthesis Services Gene Synthesis Service Custom Chemical Synthesis Other Posts: Phospho-specific antibodies by LifeTein published in Nature Synthesis of multiple antigenic peptides: strategies and limitations The Structural Basis of Peptide-Protein Binding Strategies Synthetic Peptides Used for indirect ELISAThe post LifeTein Peptide Cited in Cell first appeared on LifeTein Peptide Blog.

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How do peptides fold?

Short Peptide Folding

LifeTein Peptide Cited in Cell

Peptide by LifeTein Cited in Cell