(S)-2-Aminoundecanoic acid
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(S)-2-Aminoundecanoic acid

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Category
L-Amino Acids
Catalog number
BAT-006633
CAS number
1254251-27-8
Molecular Formula
C11H23NO2
Molecular Weight
201.31
(S)-2-Aminoundecanoic acid
IUPAC Name
(2S)-2-aminoundecanoic acid
Synonyms
H-Aund(2)-OH
Purity
95%
Density
1.0±0.1 g/cm3
Boiling Point
317.0±25.0 °C at 760 mmHg
InChI
InChI=1S/C11H23NO2/c1-2-3-4-5-6-7-8-9-10(12)11(13)14/h10H,2-9,12H2,1H3,(H,13,14)/t10-/m0/s1
InChI Key
HASUJDLTAYUWCO-JTQLQIEISA-N
Canonical SMILES
CCCCCCCCCC(C(=O)O)N
1. Chemical and Biological Characteristics of Antimicrobial α-Helical Peptides Found in Solitary Wasp Venoms and Their Interactions with Model Membranes
Marcia Perez Dos Santos Cabrera, Marisa Rangel, João Ruggiero Neto, Katsuhiro Konno Toxins (Basel). 2019 Sep 24;11(10):559. doi: 10.3390/toxins11100559.
Solitary wasps use their stinging venoms for paralyzing insect or spider prey and feeding them to their larvae. We have surveyed bioactive substances in solitary wasp venoms, and found antimicrobial peptides together with some other bioactive peptides. Eumenine mastoparan-AF (EMP-AF) was the first to be found from the venom of the solitary eumenine wasp Anterhynchium flavomarginatum micado, showing antimicrobial, histamine-releasing, and hemolytic activities, and adopting an α-helical secondary structure under appropriate conditions. Further survey of solitary wasp venom components revealed that eumenine wasp venoms contained such antimicrobial α-helical peptides as the major peptide component. This review summarizes the results obtained from the studies of these peptides in solitary wasp venoms and some analogs from the viewpoint of (1) chemical and biological characterization; (2) physicochemical properties and secondary structure; and (3) channel-like pore-forming properties.
2. Synthetic analogs of anoplin show improved antimicrobial activities
Jens K Munk, Lars Erik Uggerhøj, Tanja J Poulsen, Niels Frimodt-Møller, Reinhard Wimmer, Nils T Nyberg, Paul R Hansen J Pept Sci. 2013 Nov;19(11):669-75. doi: 10.1002/psc.2548. Epub 2013 Sep 9.
We present the antimicrobial and hemolytic activities of the decapeptide anoplin and 19 analogs thereof tested against methicillin-resistant Staphylococcus aureus ATCC 33591 (MRSA), Escherichia coli (ATCC 25922), Pseudomonas aeruginosa (ATCC 27853), vancomycin-resistant Enterococcus faecium (ATCC 700221) (VRE), and Candida albicans (ATCC 200955). The anoplin analogs contain substitutions in amino acid positions 2, 3, 5, 6, 8, 9, and 10. We use these peptides to study the effect of altering the charge and hydrophobicity of anoplin on activity against red blood cells and microorganisms. We find that increasing the charge and/or hydrophobicity improves antimicrobial activity and increases hemolytic activity. For each strain tested, we identify at least six anoplin analogs with an improved therapeutic index compared with anoplin, the only exception being Enterococcus faecium, against which only few compounds are more specific than anoplin. Both 2Nal(6) and Cha(6) show improved therapeutic index against all strains tested.
3. Novel method to identify the optimal antimicrobial peptide in a combination matrix, using anoplin as an example
J K Munk, C Ritz, F P Fliedner, N Frimodt-Møller, P R Hansen Antimicrob Agents Chemother. 2014;58(2):1063-70. doi: 10.1128/AAC.02369-13. Epub 2013 Nov 25.
Microbial resistance is an increasing health concern and a true danger to human well-being. A worldwide search for new compounds is ongoing, and antimicrobial peptides are promising lead candidates for tomorrow's antibiotics. The decapeptide anoplin (GLLKRIKTLL-NH2) is an especially interesting candidate because of its small size as well as its antimicrobial and nonhemolytic properties. Optimization of the properties of an antimicrobial peptide such as anoplin requires multidimensional searching in a complex chemical space. Typically, such optimization is performed by labor-intensive and costly trial-and-error methods. In this study, we show the benefit of fractional factorial design for identification of the optimal antimicrobial peptide in a combination matrix. We synthesized and analyzed a training set of 12 anoplin analogs, representative of 64 analogs in total. Using MIC, hemolysis, and high-performance liquid chromatography retention time data, we constructed analysis-of-variance models that describe the relationship between these properties and the structural characteristics of the analogs. We show that the mathematical models derived from the training set data can be used to predict the properties of other analogs in the chemical space. Hence, this method provides an efficient means of identification of the optimal peptide in the searched chemical space.
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