Based off of research such as this on opuntia and Echinopsis pachanoi, plus assuming they are similar too. Combined with the accounts of traditional medicine in Peru using San Pedro for such things, this sounds like a major thing that very few have realized what this means when reading the research (which you need deepdyve access or some way to search/read the full papers, it's just full of stuff they cannot profit off of so it's just talked about, science is so slow).
https://chemistry-europe...i/10.1002/cbic.201402704https://pubmed.ncbi.nlm.nih.gov/25821084/ https://www.ncbi.nlm.nih...pmc/articles/PMC8085091/ (shows how the above can be used)
https://pubmed.ncbi.nlm.nih.gov/24650181/https://www.hindawi.com/journals/jfq/2017/3075907/https://www.mdpi.com/2223-7747/10/7/1312/htmIt actually sounds so amazing:
"Naturally occurring cystine knot peptides show a wide range of biological activity, and as they have inherent stability they represent potential scaffolds for peptide-based drug design and biomolecular engineering. Here we report the discovery, sequencing, chemical synthesis, three-dimensional solution structure determination and bioactivity of the first cystine knot peptide from Cactaceae (cactus) family: Ep-AMP1 from Echinopsis pachanoi. The structure of Ep-AMP1 (35 amino acids) conforms to that of the inhibitor cystine knot (or knottin) family but represents a novel diverse sequence; its activity was more than 500 times higher against bacterial than against eukaryotic cells. Rapid bactericidal action and liposome leakage implicate membrane permeabilisation as the mechanism of action. Sequence homology places Ec-AMP1 in the plant C6-type of antimicrobial peptides, but the three dimensional structure is highly similar to that of a spider neurotoxin."
Knottin-type peptides:
"Plant knottins, which were first discovered 20 years ago and contain approximately 30 amino acids, are a superfamily that includes inhibitors of the α-amylase, carboxypeptidase, and trypsin families, as well as cyclic peptides (Le Nguyen et al. 1990). Generally, knottin-type peptides are the smallest in size among plant AMPs. They can bind to a variety of molecular targets and have multiple biological functions, such as promoting resistance to biotic and abiotic stresses, stimulating root growth, acting as signaling molecules, and enhancing symbiotic interactions. They also possess antimicrobial activity against bacteria, fungi, and viruses and even show cytotoxic, insecticidal, and anti-HIV activities (Aboye et al. 2015; Hwang et al. 2010a, b; Pallaghy et al. 1994). The typical structure of knottins involves conserved disulfide bonds between multiple cysteine pairs, forming a cystine knot (Fig. 2d). The cystine motifs of plant knottins differ within different subfamilies. In different organisms, some functionally unrelated protein families have similar knottin structures. In plants, proteins such as defensins and protease inhibitors also have cystine motifs similar to those in knottin-type peptides (Gelly et al. 2004). Although plant defensins also contain a cystine-knotting motif, they differ from knottin-like peptides in their cysteine spacing (Tam et al. 2015)."
And Peptides are amazing:
Quote:In addition, with the increasing resistance of various pathogenic bacteria to common antibiotics, there are some plant AMPs that continue to be beneficial in the treatment of various fatal human diseases. Therefore, the application of AMPs in the treatment of diseases in the medical field is receiving increasing attention.
Sources of antimicrobial peptides from the antimicrobial peptide database (http://aps.unmc.edu/AP/)
Classification of plant AMPs
The composition of plant AMPs is very complex. A single plant species can contain a variety of AMPs (Noonan et al. 2017). Most plant AMPs are positively charged at physiological pH with molecular weights ranging from 2–10 kDa. AMPs contain 4–12 cysteine residues forming disulfide bonds, which can make them exceptionally stable to chemical, thermal and enzymatic degradation by stabilizing their tertiary and quaternary structures (Faull et al. 2020; Khoo et al. 2011; Sohail et al. 2020; Tam et al. 2015). The smallest known AMP comprising seven amino acids (Lys-Val-Phe-Leu-Gly-Leu-Lys) was isolated from Jatropha curcas (Xiao et al. 2011). Plant AMPs have diverse functions, structures, and expression patterns, as well as specific targets, which make their classification more complex and difficult. Plant AMPs can be classified into cationic peptides and anionic peptides according to their charge (Hammami et al. 2009; Prabhu et al. 2014). However, the classifications of plant AMPs are usually based on their sequence similarity, presence of cysteine motifs, and tertiary structures (Hammami et al. 2009) (Table (Table11).
Summary of some common plant antimicrobial peptides about their classification and Bioactivities
Peptide Classification Function Potency Refs.
Ep-AMP1 Knottin-type peptides Antibacterial, Antifungal 0.31–10e Aboye et al, 2015
As for preparation in general it's just like CBD topicals for recipes but not exactly as easy since more water based. I have pondered a DMSO based topical to increase absorption. I think this full spectrum extract has many uses similar to cannabis topical and more hopefully too in many medicinal ways as future research comes out.