Epinecidin-1 & Temporin-Shx
Antimicrobial Peptides (AMP)
| Peptidname | L-AA-Sequenz; Gegenion: TFA, >80% Reinheit, Menge: 2 mg | Price (without VAT, netto) **) |
|---|---|---|
| Epinecidin-1 | GFIFHIIKGLFHAGKMIHGLV (21-mer) https://www.frontiersin.org/articles/10.3389/fmicb.2019.02631/full | 155,30 € |
| Sha | FLSGIVGMLGKLF (Two temporins, temporin-SHa and temporin-SHd, found in the skin secretions of the North African ranid frog Pelophylax saharicus, also target efficiently Gram-negative bacteria. However, with only 13 amino acid residues, temporin-SHa has a much broader spectrum, compared to temporin-SHd (17 amino acid residues), being potent against E. coli and A. baumannii, S. enterica serovar Enteritidis and K. pneumoniae.) | 149,90 € |
| **) Bei Angabe der USt.-ID Nummer ist der Angebotspreis auch gleich Rechnungsbetrag (netto = brutto). | Bitte fügen Sie bei Ihrer Bestellung die Peptidsequenz, Menge, Reinheit und Preisangabe einfach per copy + paste ein. |
Marine Peptide
“The Antimicrobial Peptide Database” and among them 125 originated from fish
https://aps.unmc.edu/AP/
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4515606/
The majority of work studying the potential pharmacological activities of epinecidin-1, utilize synthesized epinecidin-1 (Epi-1), which is made up of 21 amino acids, from the amino acid sequence of 22–42 residues of Epi-1—GFIFHIIKGLFHAGKMIHGLV. The synthetized Epi-1 peptide has been demonstrated to possess diverse pharmacological activities, including antimicrobial, immunomodulatory, anticancer, and wound healing properties.
Thanatin Peptide
| Peptidname | L-AA-Sequenz; Gegenion: Acetat, >95% Reinheit, Menge: 5 mg | Price (without VAT, netto) **) |
| Thanatin Molecular Weight (MW) 2433.96 g/mol |
Sequence GSKKPVPIIYCNRRTGKCQRM (21mer) Modification disulfide bond: Cys11-Cys18 |
789,30 € |
| **) Bei Angabe der USt.-ID Nummer ist der Angebotspreis auch gleich Rechnungsbetrag (netto = brutto). |
TAT peptides
TAT peptides are cell penetrating peptides derived from the trans-activating transcriptional activator (Tat) from HIV-1 like : [(Y)GRKKRRQRRRPQ) + choose your individual amino acid sequence ] .
Antimikrobielle Peptide (AMP)
Given the low bioavailability of relevant AMPs in nature, biotechnological interventions with genetic engineering and synthetic biology strategies for enhanced AMP synthesis have been a key focus in industry [1]. With this, as synthetic peptide development approaches have improved, the potential of synthetic AMPs to counteract pathogens and emerging infections has grown – they can now be designed with multifaceted mechanisms of action and act as antiviral, antibacterial and antifungal agents.
Key categories of AMPs currently in development include receptor-binding peptides, membrane-active peptides, membrane-lytic peptides and inhibitory peptides (such as cell wall-inhibiting peptides) [2]. AMPs generally affect highly preserved structures and can be used against specific targets such as peptidoglycans in Gram-negative and Gram-positive bacteria, and glucan in the fungal cell wall. Other peptides are particularly active on biofilm destabilizing the microbial communities. Synthetic peptides have also been marked as a potential solution to help combat antibiotic-resistant microbes such as drug-resistant Staphylococcus aureus. They can also act intracellularly – for instance, on protein biosynthesis or DNA replication [3].
As well as mimicking pharmacological properties, structural and amino acid sequence improvements can also be used to address challenges associated with natural AMPs, such as instability when used as a drug, host toxicity, rapid degradation by proteases and loss of activity in presence of serum and high salt concentrations [2,3]. Short-sequence AMPs (<20 amino acids) can be used to combine optimal antimicrobial activity with inexpensive chemical synthesis and modifications required to ensure stability, low toxicity and microbial specificity, and are compatible with large-scale production [4]. Mesh: #Antimicrobial #Peptides
DOPA-Spacer-AMP
https://www.mpg.de/muschelprotein-selbstheilung
"Die Forscher aus Potsdam enthüllten, dass die Außenhaut aus einem Proteinnetz besteht, welches durch Komplexe aus Eisenmolekülen und L-DOPA, einer veränderten Form der Aminosäure Tyrosin, stabilisiert wird. Ein einziges Eisen-Ion kann an bis zu drei DOPA-Moleküle binden, so dass ein äußerst stabiler Metallproteinkomplex entsteht. Eine solche Bindung aufzubrechen, ist schwer und kostet fast soviel Energie wie eine kovalente Bindung zwischen zwei Atomen. Die Metall-DOPA-Bindung ist ähnlich stabil, hat aber einen entscheidenden Vorteil: Im Gegensatz zur Atombindung kann sie sich spontan wieder bilden, nachdem sie gebrochen ist. So könnten winzige Risse in der Hülle von selbst heilen, wie die Forscher vermuten. Solche Risse entstehen etwa, wenn der Byssus überdehnt wird. Sie nehmen einen Teil der Dehnungsenergie auf, so dass der Faden nicht komplett abreißt. (Stand: 2011)
Cu-AMP-DOPA
Ga-AMP-DOPA
pen-Spacer-AMP
Pencillinamine, [pen]
Literatur
1. Sinha, R. & Dhukla, P. Antimicrobial Peptides: Recent Insights on Biotechnological Interventions and Future Perspectives. Protein & Peptide Letters 26, 79-87 (2019).
2. Chen, C. H. & Lu, T. Development and Challenges of Antimicrobial Peptides for Therapeutic Applications. Antibiotics 10.3390/antibiotics9010024 (2020).
3. Vanzolini, T. et al. Multitalented synthetic antimicrobial peptides and their antibacterial, antifungal and antiviral mechanisms. Int. J. Mol. Sci. 23, 545 (2022).
4. Rahnamaeian, M. & Vileinskas, A. Short antimicrobial peptides as cosmetic ingredients to deter dermatological pathogens. Appl. Microbiol. Biotechnol. 99, 8847–8855 (2015).
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