L-Isoleucine is an essential branched-chain amino acid (BCAA) that plays a critical role in protein synthesis and energy production. It is one of the 20 standard amino acids used by cells to synthesize proteins. Characteristically, L-Isoleucine is hydrophobic, which influences its role in protein structure and function. It has a side chain that contains an isopropyl group, contributing to its non-polar nature. This amino acid is vital for muscle metabolism and is involved in regulating blood sugar levels and energy production. The compound you mentioned appears to be a complex peptide sequence that includes multiple repetitions of L-Isoleucine along with other amino acids such as L-arginine, L-leucine, L-alanine, and L-glutamine. Such sequences can exhibit unique biological activities and may be of interest in research related to peptide synthesis, therapeutic applications, or nutritional supplementation. However, the specific properties and functions of this complex peptide would depend on its structure and the arrangement of its constituent amino acids.

L-Isoleucine, L-isoleucyl-L-arginyl-L-isoleucyl-L-isoleucyl-L-leucyl-L-arginyl-L-alanyl-L-glutaminylglycyl-L-alanyl-L-leucyl-L-lysyl-

2396407-35-3: L-Isoleucine is an essential branched-chain amino acid (BCAA) that plays a critical role in protein synthesis and energy production. It is one of the 20 standard amino acids used by cells to synthesize proteins. Characteristically, L-Isoleucine is hydrophobic, which influences its role in protein structure and function. It has a side chain that contains an isopropyl group, contributing to its non-polar nature. This amino acid is vital for muscle metabolism and is involved in regulating blood sugar levels and energy production. The compound you mentioned appears to be a complex peptide sequence that includes multiple repetitions of L-Isoleucine along with other amino acids such as L-arginine, L-leucine, L-alanine, and L-glutamine. Such sequences can exhibit unique biological activities and may be of interest in research related to peptide synthesis, therapeutic applications, or nutritional supplementation. However, the specific properties and functions of this complex peptide would depend on its structure and the arrangement of its constituent amino acids.

<p>BING is an antimicrobial peptide isolated from Japanese medaka fish. It exhibits broad-spectrum toxicity against pathogenic bacteria, including resistant strains. BING disrupts the periplasmic peptidyl-prolyl isomerase in Gram-negative bacteria and reduces RNA levels of cpxR, which plays a crucial role in the development of antibiotic resistance.</p>

CAS 2396407-35-3

L-Isoleucine, L-isoleucyl-L-arginyl-L-isoleucyl-L-isoleucyl-L-leucyl-L-arginyl-L-alanyl-L-glutaminylglycyl-L-alanyl-L-leucyl-L-lysyl-

BING

Ref: TM-TP2706