The RGD peptide is critical for the establishment of the extracellular matrix of animal cells. a. Draw the structure of the RGD peptide at physiological pH (pH = 7). b. What is the charge of this peptide at physiological pH? At high pH (pH > 13)? Low pH (pH < 3)?

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### The Significance of the RGD Peptide in the Extracellular Matrix of Animal Cells

The RGD (Arginine-Glycine-Aspartic acid) peptide plays a vital role in the formation and function of the extracellular matrix in animal cells. This short sequence of amino acids is recognized by cell surface receptors and is crucial for cell adhesion, migration, and signaling.

#### Discussion Points

a. **Structure of the RGD Peptide at Physiological pH (pH = 7):**

- At physiological pH, the RGD peptide structure should include the side chains of the amino acids involved:
  - **Arginine (R)** has a positively charged side chain at physiological pH.
  - **Glycine (G)** is neutral, with no side chain beyond a single hydrogen atom.
  - **Aspartic acid (D)** has a negatively charged side chain at physiological pH.

b. **Charge of the RGD Peptide at Various pH Levels:**

- **At Physiological pH (pH = 7):** The overall charge of the RGD peptide results from its constituent amino acids. Typically, the charge is neutralized by the balancing positive and negative charges of arginine and aspartic acid.
  
- **At High pH (pH > 13):** At this alkaline pH, the carboxyl groups may lose protons, giving the peptide an overall charged state, often negatively charged due to the deprotonation of acidic side chains.

- **At Low pH (pH < 3):** In a highly acidic environment, the amino groups are more likely to retain protons, which can lead to a more positive charge on the peptide due to the protonation of basic side chains like that of arginine.

This understanding of pH-dependent charge states is essential for analyzing how the RGD peptide behaves under different physiological conditions, affecting its role in cellular interactions and the extracellular matrix.
Transcribed Image Text:### The Significance of the RGD Peptide in the Extracellular Matrix of Animal Cells The RGD (Arginine-Glycine-Aspartic acid) peptide plays a vital role in the formation and function of the extracellular matrix in animal cells. This short sequence of amino acids is recognized by cell surface receptors and is crucial for cell adhesion, migration, and signaling. #### Discussion Points a. **Structure of the RGD Peptide at Physiological pH (pH = 7):** - At physiological pH, the RGD peptide structure should include the side chains of the amino acids involved: - **Arginine (R)** has a positively charged side chain at physiological pH. - **Glycine (G)** is neutral, with no side chain beyond a single hydrogen atom. - **Aspartic acid (D)** has a negatively charged side chain at physiological pH. b. **Charge of the RGD Peptide at Various pH Levels:** - **At Physiological pH (pH = 7):** The overall charge of the RGD peptide results from its constituent amino acids. Typically, the charge is neutralized by the balancing positive and negative charges of arginine and aspartic acid. - **At High pH (pH > 13):** At this alkaline pH, the carboxyl groups may lose protons, giving the peptide an overall charged state, often negatively charged due to the deprotonation of acidic side chains. - **At Low pH (pH < 3):** In a highly acidic environment, the amino groups are more likely to retain protons, which can lead to a more positive charge on the peptide due to the protonation of basic side chains like that of arginine. This understanding of pH-dependent charge states is essential for analyzing how the RGD peptide behaves under different physiological conditions, affecting its role in cellular interactions and the extracellular matrix.
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