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  • HLopt2 peptide

HLopt2 peptide

Cat.#: 318808

Optional Service: TFA RemovalWhat's this?

Special Price 94.5 USD

Availability: 1-2 weeks
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Product Information

  • Product Name
    HLopt2 peptide
  • Documents
  • Quantity/Unit
    1 Vial
  • Sequence
  • Three letter code
  • Length (aa)
  • Peptide Purity (HPLC)
  • Molecular Formula
  • Molecular Weight
  • Source
  • Additional Information
    Owing to the increasing number of infections in hospitalised patients caused by resistant strains of fungi, there is a need to develop new therapeutic agents for these infections. Naturally occurring antimicrobial peptides may constitute models for developing such agents. A modified peptide sequence (CFQWKRAMRKVR; HLopt2) based on amino acid residues 20–31 of the N-terminal end of human lactoferrin (hLF) as well as a double-sized human lactoferricin-like peptide (amino acid residues 16–40; HLBD1) were investigated for their antifungal activities in vitro and in vivo. By in vitro assay, HLopt2 was fungicidal at concentrations of 12.5–25 μg/mL against Cryptococcus neoformans, Candida albicans, Candida krusei, Candida kefyr and Candida parapsilosis, but not against Candida glabrata. HLopt2 was demonstrated to have ≥16-fold greater killing activity than HLBD1. By inducing some helical formation caused by lactam bridges or by extending the assay time (from 2 h to 20 h), HLBD1 became almost comparable with HLopt2 in its fungicidal activity. Killing of C. albicans yeast cells by HLopt2 was rapid and was accompanied by cytoplasmic and mitochondrial membrane permeabilisation as well as formation of deep pits on the yeast cell surface. In a murine C. albicans skin infection model, atopic treatment with the peptides resulted in significantly reduced yields of Candida from the infected skin areas. The antifungal activities of HLopt2 in vitro and in vivo suggest possible potential as a therapeutic agent against most Candida spp. and C. neoformans. The greatly improved antifungal effect of the lactam-modified HLBD1 indicates the importance of amphipathic helix formation for lethal activity.
  • Storage Guidelines
    Ideally HLopt2 peptide should be stored in a freezer at or below -9C. HLopt2 peptide should be refrigerated after reconstitution. For more details, please refer to the manual:Handling and Storage of Synthetic Peptides
  • References
    • Kondori N, Baltzer L, Dolphin GT, Mattsby-Baltzer I. Fungicidal activity of human lactoferrin-derived peptides based on the antimicrobial u03b1u03b2 region. Int J Antimicrob Agents. 2011;37(1):51u201357. doi:10.1016/j.ijantimicag.2010.08.020
  • About TFA salt

    Trifluoroacetic acid (TFA) is a strong acid, which is commonly used to cleave synthesized peptides from solid-phase resins and is also used to improve HPLC performance in the peptide purification step. By default, custom peptides are delivered as lyophilized TFA salts, and can contain as much as 10-45% TFA.

    TFA in custom peptides can cause inexplicable discrepancies in subsequent assay data. For instance, TFA in nM concentrations has been shown to interfere with cellular assays, inhibiting cellular proliferation in some instances, and increasing cell viability in others . It has also been found to be an unintended allosteric modulator of the glycine receptor, GlyR.

    TFA Removal Service is recommended for:

    • Peptides that will be used in cellular assays
    • Peptides that will be used as APIs or in manufactured products
    • For hydrophilic peptides containing numerous basic residues

Peptide Property

Peptide Services: NovoPro's peptide synthesis services include standard chemical peptide synthesis, peptide modification, peptide libraries, and recombinant peptide expression.

Standard Peptide Synthesis: NovoPro offers quality peptides at the most competitive prices in the industry, starting at $3.20 per amino acid. NovoPro provides PepBox – Automatic Quote Tool for online price calculation.

Peptide Modifications: NovoPro offers a wide range of peptide modification services including isotope labeling (2H, 15N, and 13C), multiple disulfide bonds, multiple phosphorylations, KLH, BSA, ovalbumin, amidation, acetylation, biotin, FITC, etc.