Sequence Determination of the Brain Peptide Leucine Enkephalin A group of peptides that influence nerve transmission in certain parts of the brain has been isolated from normal brain tissue. These peptides are known as opioids, because they bind to specific receptors that also bind opiate drugs, such as morphine and naloxone. Opioids thus mimic some of the properties of opiates. Some researchers consider these peptides to be the brain�s own pain killers. Using the information below, determine the amino acid sequence of the opioid leucine enkephalin. Explain how your structure is consistent with each piece of information.(a) Complete hydrolysis by 6 M HCl at 110 C followed by amino acid analysis indicated the presence of Gly, Leu,Phe, and Tyr, in a 2:1:1:1 molar ratio.(b) Treatment of the peptide with 1-fluoro-2,4-dinitrobenzene followed by complete hydrolysis and chromatography indicated the presence of the 2,4-dinitrophenyl derivative of tyrosine. No free tyrosine could be found.(c) Complete digestion of the peptide with chymopepsin followed by chromatography yielded free tyrosine and leucin plus a tripeptide containing Phe and Gly in a 1:2 ratio.

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12-12-2022
Chemistry

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Sequence Determination of the Brain Peptide Leucine Enkephalin A group of peptides that influence nerve transmission in certain parts of the brain has been isolated from normal brain tissue. These peptides are known as opioids, because they bind to specific receptors that also bind opiate drugs, such as morphine and naloxone. Opioids thus mimic some of the properties of opiates. Some researchers consider these peptides to be the brain�s own pain killers. Using the information below, determine the amino acid sequence of the opioid leucine enkephalin. Explain how your structure is consistent with each piece of information.(a) Complete hydrolysis by 6 M HCl at 110 C followed by amino acid analysis indicated the presence of Gly, Leu,Phe, and Tyr, in a 2:1:1:1 molar ratio.(b) Treatment of the peptide with 1-fluoro-2,4-dinitrobenzene followed by complete hydrolysis and chromatography indicated the presence of the 2,4-dinitrophenyl derivative of tyrosine. No free tyrosine could be found.(c) Complete digestion of the peptide with chymopepsin followed by chromatography yielded free tyrosine and leucin plus a tripeptide containing Phe and Gly in a 1:2 ratio.

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fawadmohd fawadmohd · Answer 1 · 2022-12-18T01:43:36-05:00

Option C) "are digested by proteases into both opiate and non-opiate peptides" is the correct response.

Like all other propeptides, the opioid propeptides is a protein precursor that must be cut into a smaller form to become active. Proteases convert the opioid propeptides into opiate and non-opiate peptides, the latter of which may or may not be active. Enkephalins, endorphins, and dynorphins, which are opiate peptides, work by blocking secondary systems, such as those that affect how pain is perceived.

The opioid receptors are essential signalling molecules in the brain that the leucine-enkephalin binds to. They include four peptide bonds in total. These are naturally occurring ligands that function as neurotransmitters and have morphine-like properties.

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