Part:BBa_K5185015

CBM5-sumo-HNP1

CBM5-sumo-HNP1 is a fusion protein combining three distinct domains: Human Neutrophil Peptide 1 (HNP1BBa_K5185000 ), a natural antimicrobial peptide belonging to the alpha defensin family that exhibits antimicrobial activity against Gram-positive and Gram-negative bacteria, fungi, and certain enveloped viruses, Carbonhydrate-Binding molecule 5(CBM5 BBa_K5185002), which enhances the targeting of chitosan-containing materials for modification or degradation, and the SUMO tag No part name specified with partinfo tag., which can improve the solubility, stability, and folding of proteins. The universality of the combined function of the binding domain and defensins of this part is assessed. The fusion protein allowing for a more versatile collection of antibacterial dressings and enhanced potential of our first aid kit to address more complex situations.

CBM5-sumo-HNP1 is a fusion protein with three distinct domains: Human Neutrophil Peptide 1 (HNP1, BBa_K5185000), a natural antimicrobial peptide belonging to the α-defensin family that exhibits antimicrobial activity against Gram-positive and Gram-negative bacteria, fungi, and certain enveloped viruses, Carbonhydrate-Binding molecule 5 (CBM5 BBa_K5185002)that allows the defensin to attach to chitosan-containing materials of the first aid kit, and the SUMO tag (BBa_K4170016) which improves the solubility, stability, and folding of proteins. This part is part of a collection where the universality of the combined function of the binding domain and defensins is assessed, allowing for a more versatile collection of antibacterial dressings and enhancing the potential of our first aid kit to address more complex situations.

Our project aims to endow first-aid wound dressings with enhanced antimicrobial functions and a wider and more complex application. By fusing the binding domain CBM5 with the defensin HNP1, we can bestow items such as bandages and antiseptic wipes, specifically those made of chitosan, with properties that facilitate hemostasis and prevents bacterial growth. CBM5 allows the HNP to attach to chitosan-containing materials, while HNP1 interferes with the normal functionality of bacteria.

This is part of a part collection of SUMO linking a binding domain to defensin, which allows defensins to be attached to carbohydrates such as cellulose, chitosan, and collagen. When applied with a SUMO Protease, this fusion protein may effectively release the defensin into the site of injury and therefore achieve the desired antimicrobial effects, acting as a reliable defense against bacterial infections while mitigating the growing concern of antibiotic resistance.

Other than CBM5, this part collection includes other CBMs such as CBM2, CBM3, and VbCBMxx, and also human integrin domains such as α1 and α2. Other than HNP1, other defensins in this part collection include HNP4, HD5, and HBD3. We synthesized the fusion proteins CBM3-sumo-HNP1 (BBa_K5185010), CBM3-sumo-HNP4 (BBa_K5185011),CBM3-sumo-HD5 (BBa_K5185012), and CBM3-sumo-HBD3 (BBa_K5185013) for materials in the first aid kit composed of cellulose, bestowing them with antimicrobial functions. Other fusion proteins we synthesized include CBM5-sumo-HNP1 (BBa_K5185015) which focuses on more enhanced anti-microbial functions and targets especially severe infections, and α2-sumo-HNP1 (BBa_K5185017) which with the use of collagen enables better wound healing, targeting wounds that prioritize wound recovery. Recognizing this part collection of fusion proteins as effective in treating wounds and achieving antimicrobial needs, we believe the HNPs could each be linked with different wound-dressing materials that would provide an array of approaches and solutions to suit the varied needs of different wounds and circumstances with limited medical resources, such as battlefields and disaster zones.

Sequence and Features

Assembly Compatibility:

• 10
  COMPATIBLE WITH RFC[10]
• 12
  COMPATIBLE WITH RFC[12]
• 21
  COMPATIBLE WITH RFC[21]
• 23
  COMPATIBLE WITH RFC[23]
• 25
  INCOMPATIBLE WITH RFC[25]

  Illegal NgoMIV site found at 61
  Illegal NgoMIV site found at 126
  
• 1000
  COMPATIBLE WITH RFC[1000]